JPH03148624A - Method and device for washing - Google Patents
Method and device for washingInfo
- Publication number
- JPH03148624A JPH03148624A JP28754989A JP28754989A JPH03148624A JP H03148624 A JPH03148624 A JP H03148624A JP 28754989 A JP28754989 A JP 28754989A JP 28754989 A JP28754989 A JP 28754989A JP H03148624 A JPH03148624 A JP H03148624A
- Authority
- JP
- Japan
- Prior art keywords
- cleaning
- cleaned
- electrophoretic
- washing
- hydrophilic gel
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 238000000034 method Methods 0.000 title claims description 23
- 238000005406 washing Methods 0.000 title abstract description 13
- 230000000694 effects Effects 0.000 claims abstract description 15
- 239000007788 liquid Substances 0.000 claims abstract description 15
- 238000001962 electrophoresis Methods 0.000 claims abstract description 9
- 150000002500 ions Chemical class 0.000 claims abstract description 6
- 239000000084 colloidal system Substances 0.000 claims abstract 5
- 238000004140 cleaning Methods 0.000 claims description 69
- 238000001816 cooling Methods 0.000 claims description 9
- 108090000790 Enzymes Proteins 0.000 claims description 7
- 102000004190 Enzymes Human genes 0.000 claims description 7
- 229940088598 enzyme Drugs 0.000 claims description 7
- -1 polyethylene Polymers 0.000 claims description 7
- 239000002253 acid Substances 0.000 claims description 6
- 239000000243 solution Substances 0.000 claims description 6
- 239000003513 alkali Substances 0.000 claims description 5
- 238000003780 insertion Methods 0.000 claims description 5
- 230000037431 insertion Effects 0.000 claims description 5
- 238000002604 ultrasonography Methods 0.000 claims description 4
- 102000013142 Amylases Human genes 0.000 claims description 3
- 108010065511 Amylases Proteins 0.000 claims description 3
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 3
- 108091005804 Peptidases Proteins 0.000 claims description 3
- 102000035195 Peptidases Human genes 0.000 claims description 3
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 claims description 3
- 239000012670 alkaline solution Substances 0.000 claims description 3
- 230000000593 degrading effect Effects 0.000 claims description 3
- 230000005611 electricity Effects 0.000 claims description 3
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 claims description 3
- 235000019333 sodium laurylsulphate Nutrition 0.000 claims description 3
- BHQCQFFYRZLCQQ-UHFFFAOYSA-N (3alpha,5alpha,7alpha,12alpha)-3,7,12-trihydroxy-cholan-24-oic acid Natural products OC1CC2CC(O)CCC2(C)C2C1C1CCC(C(CCC(O)=O)C)C1(C)C(O)C2 BHQCQFFYRZLCQQ-UHFFFAOYSA-N 0.000 claims description 2
- QZPSOSOOLFHYRR-UHFFFAOYSA-N 3-hydroxypropyl prop-2-enoate Chemical compound OCCCOC(=O)C=C QZPSOSOOLFHYRR-UHFFFAOYSA-N 0.000 claims description 2
- 229920000049 Carbon (fiber) Polymers 0.000 claims description 2
- 239000004380 Cholic acid Substances 0.000 claims description 2
- 108090001069 Chymopapain Proteins 0.000 claims description 2
- 108090000317 Chymotrypsin Proteins 0.000 claims description 2
- 102100026735 Coagulation factor VIII Human genes 0.000 claims description 2
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 claims description 2
- WOBHKFSMXKNTIM-UHFFFAOYSA-N Hydroxyethyl methacrylate Chemical compound CC(=C)C(=O)OCCO WOBHKFSMXKNTIM-UHFFFAOYSA-N 0.000 claims description 2
- 108090000526 Papain Proteins 0.000 claims description 2
- 239000004698 Polyethylene Substances 0.000 claims description 2
- 239000004743 Polypropylene Substances 0.000 claims description 2
- 239000004365 Protease Substances 0.000 claims description 2
- ISWQCIVKKSOKNN-UHFFFAOYSA-L Tiron Chemical compound [Na+].[Na+].OC1=CC(S([O-])(=O)=O)=CC(S([O-])(=O)=O)=C1O ISWQCIVKKSOKNN-UHFFFAOYSA-L 0.000 claims description 2
- 108090000631 Trypsin Proteins 0.000 claims description 2
- 102000004142 Trypsin Human genes 0.000 claims description 2
- 239000003945 anionic surfactant Substances 0.000 claims description 2
- 239000007864 aqueous solution Substances 0.000 claims description 2
- 239000004917 carbon fiber Substances 0.000 claims description 2
- 239000002738 chelating agent Substances 0.000 claims description 2
- 235000019416 cholic acid Nutrition 0.000 claims description 2
- BHQCQFFYRZLCQQ-OELDTZBJSA-N cholic acid Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 BHQCQFFYRZLCQQ-OELDTZBJSA-N 0.000 claims description 2
- 229960002471 cholic acid Drugs 0.000 claims description 2
- 229960002976 chymopapain Drugs 0.000 claims description 2
- 229960002376 chymotrypsin Drugs 0.000 claims description 2
- 239000000498 cooling water Substances 0.000 claims description 2
- KXGVEGMKQFWNSR-UHFFFAOYSA-N deoxycholic acid Natural products C1CC2CC(O)CCC2(C)C2C1C1CCC(C(CCC(O)=O)C)C1(C)C(O)C2 KXGVEGMKQFWNSR-UHFFFAOYSA-N 0.000 claims description 2
- 229940111205 diastase Drugs 0.000 claims description 2
- 235000014113 dietary fatty acids Nutrition 0.000 claims description 2
- 150000002148 esters Chemical class 0.000 claims description 2
- 239000000194 fatty acid Substances 0.000 claims description 2
- 229930195729 fatty acid Natural products 0.000 claims description 2
- 150000004665 fatty acids Chemical class 0.000 claims description 2
- 235000011389 fruit/vegetable juice Nutrition 0.000 claims description 2
- 210000004185 liver Anatomy 0.000 claims description 2
- 229910052751 metal Inorganic materials 0.000 claims description 2
- 239000002184 metal Substances 0.000 claims description 2
- VNWKTOKETHGBQD-UHFFFAOYSA-N methane Chemical compound C VNWKTOKETHGBQD-UHFFFAOYSA-N 0.000 claims description 2
- GBCAVSYHPPARHX-UHFFFAOYSA-M n'-cyclohexyl-n-[2-(4-methylmorpholin-4-ium-4-yl)ethyl]methanediimine;4-methylbenzenesulfonate Chemical compound CC1=CC=C(S([O-])(=O)=O)C=C1.C1CCCCC1N=C=NCC[N+]1(C)CCOCC1 GBCAVSYHPPARHX-UHFFFAOYSA-M 0.000 claims description 2
- 230000003204 osmotic effect Effects 0.000 claims description 2
- 229940055729 papain Drugs 0.000 claims description 2
- 235000019834 papain Nutrition 0.000 claims description 2
- 239000004033 plastic Substances 0.000 claims description 2
- 229920003023 plastic Polymers 0.000 claims description 2
- 229920000573 polyethylene Polymers 0.000 claims description 2
- 229920001155 polypropylene Polymers 0.000 claims description 2
- 238000007789 sealing Methods 0.000 claims description 2
- 229960001322 trypsin Drugs 0.000 claims description 2
- 239000012588 trypsin Substances 0.000 claims description 2
- NIXOWILDQLNWCW-UHFFFAOYSA-M Acrylate Chemical compound [O-]C(=O)C=C NIXOWILDQLNWCW-UHFFFAOYSA-M 0.000 claims 1
- 239000004367 Lipase Substances 0.000 claims 1
- 102000004882 Lipase Human genes 0.000 claims 1
- 108090001060 Lipase Proteins 0.000 claims 1
- 102000015728 Mucins Human genes 0.000 claims 1
- 108010063954 Mucins Proteins 0.000 claims 1
- 238000010306 acid treatment Methods 0.000 claims 1
- 239000003599 detergent Substances 0.000 claims 1
- 235000019421 lipase Nutrition 0.000 claims 1
- 229910000510 noble metal Inorganic materials 0.000 claims 1
- 239000002736 nonionic surfactant Substances 0.000 claims 1
- 239000004094 surface-active agent Substances 0.000 abstract description 4
- 239000002245 particle Substances 0.000 abstract description 2
- 230000003287 optical effect Effects 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 238000010586 diagram Methods 0.000 description 3
- 239000011734 sodium Substances 0.000 description 3
- 229910001415 sodium ion Inorganic materials 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- PIIRYSWVJSPXMW-UHFFFAOYSA-N 1-octyl-4-(4-octylphenoxy)benzene Chemical compound C1=CC(CCCCCCCC)=CC=C1OC1=CC=C(CCCCCCCC)C=C1 PIIRYSWVJSPXMW-UHFFFAOYSA-N 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 102000016943 Muramidase Human genes 0.000 description 2
- 108010014251 Muramidase Proteins 0.000 description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000012459 cleaning agent Substances 0.000 description 2
- WQYVRQLZKVEZGA-UHFFFAOYSA-N hypochlorite Chemical compound Cl[O-] WQYVRQLZKVEZGA-UHFFFAOYSA-N 0.000 description 2
- 229960000274 lysozyme Drugs 0.000 description 2
- 239000004325 lysozyme Substances 0.000 description 2
- 235000010335 lysozyme Nutrition 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- JNYAEWCLZODPBN-JGWLITMVSA-N (2r,3r,4s)-2-[(1r)-1,2-dihydroxyethyl]oxolane-3,4-diol Chemical compound OC[C@@H](O)[C@H]1OC[C@H](O)[C@H]1O JNYAEWCLZODPBN-JGWLITMVSA-N 0.000 description 1
- LNAZSHAWQACDHT-XIYTZBAFSA-N (2r,3r,4s,5r,6s)-4,5-dimethoxy-2-(methoxymethyl)-3-[(2s,3r,4s,5r,6r)-3,4,5-trimethoxy-6-(methoxymethyl)oxan-2-yl]oxy-6-[(2r,3r,4s,5r,6r)-4,5,6-trimethoxy-2-(methoxymethyl)oxan-3-yl]oxyoxane Chemical compound CO[C@@H]1[C@@H](OC)[C@H](OC)[C@@H](COC)O[C@H]1O[C@H]1[C@H](OC)[C@@H](OC)[C@H](O[C@H]2[C@@H]([C@@H](OC)[C@H](OC)O[C@@H]2COC)OC)O[C@@H]1COC LNAZSHAWQACDHT-XIYTZBAFSA-N 0.000 description 1
- LTSWUFKUZPPYEG-UHFFFAOYSA-N 1-decoxydecane Chemical compound CCCCCCCCCCOCCCCCCCCCC LTSWUFKUZPPYEG-UHFFFAOYSA-N 0.000 description 1
- CMCBDXRRFKYBDG-UHFFFAOYSA-N 1-dodecoxydodecane Chemical compound CCCCCCCCCCCCOCCCCCCCCCCCC CMCBDXRRFKYBDG-UHFFFAOYSA-N 0.000 description 1
- FDCJDKXCCYFOCV-UHFFFAOYSA-N 1-hexadecoxyhexadecane Chemical compound CCCCCCCCCCCCCCCCOCCCCCCCCCCCCCCCC FDCJDKXCCYFOCV-UHFFFAOYSA-N 0.000 description 1
- OUUCZGCOAXRCHN-UHFFFAOYSA-N 1-hexadecoxyoctadecane Chemical compound CCCCCCCCCCCCCCCCCCOCCCCCCCCCCCCCCCC OUUCZGCOAXRCHN-UHFFFAOYSA-N 0.000 description 1
- HANWHVWXFQSQGJ-UHFFFAOYSA-N 1-tetradecoxytetradecane Chemical compound CCCCCCCCCCCCCCOCCCCCCCCCCCCCC HANWHVWXFQSQGJ-UHFFFAOYSA-N 0.000 description 1
- CSHOPPGMNYULAD-UHFFFAOYSA-N 1-tridecoxytridecane Chemical compound CCCCCCCCCCCCCOCCCCCCCCCCCCC CSHOPPGMNYULAD-UHFFFAOYSA-N 0.000 description 1
- OMIGHNLMNHATMP-UHFFFAOYSA-N 2-hydroxyethyl prop-2-enoate Chemical compound OCCOC(=O)C=C OMIGHNLMNHATMP-UHFFFAOYSA-N 0.000 description 1
- XZIIFPSPUDAGJM-UHFFFAOYSA-N 6-chloro-2-n,2-n-diethylpyrimidine-2,4-diamine Chemical compound CCN(CC)C1=NC(N)=CC(Cl)=N1 XZIIFPSPUDAGJM-UHFFFAOYSA-N 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- SNRUBQQJIBEYMU-UHFFFAOYSA-N Dodecane Natural products CCCCCCCCCCCC SNRUBQQJIBEYMU-UHFFFAOYSA-N 0.000 description 1
- 239000001856 Ethyl cellulose Substances 0.000 description 1
- ZZSNKZQZMQGXPY-UHFFFAOYSA-N Ethyl cellulose Chemical compound CCOCC1OC(OC)C(OCC)C(OCC)C1OC1C(O)C(O)C(OC)C(CO)O1 ZZSNKZQZMQGXPY-UHFFFAOYSA-N 0.000 description 1
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 1
- 102100022624 Glucoamylase Human genes 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 108010019160 Pancreatin Proteins 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 229920002125 Sokalan® Polymers 0.000 description 1
- IYFATESGLOUGBX-YVNJGZBMSA-N Sorbitan monopalmitate Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)[C@H]1OC[C@H](O)[C@H]1O IYFATESGLOUGBX-YVNJGZBMSA-N 0.000 description 1
- WDJHALXBUFZDSR-UHFFFAOYSA-N acetoacetic acid Chemical compound CC(=O)CC(O)=O WDJHALXBUFZDSR-UHFFFAOYSA-N 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 238000005034 decoration Methods 0.000 description 1
- KWKXNDCHNDYVRT-UHFFFAOYSA-N dodecylbenzene Chemical compound CCCCCCCCCCCCC1=CC=CC=C1 KWKXNDCHNDYVRT-UHFFFAOYSA-N 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 235000019325 ethyl cellulose Nutrition 0.000 description 1
- 229920001249 ethyl cellulose Polymers 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000009434 installation Methods 0.000 description 1
- 239000003014 ion exchange membrane Substances 0.000 description 1
- 239000002075 main ingredient Substances 0.000 description 1
- 229920000609 methyl cellulose Polymers 0.000 description 1
- 239000001923 methylcellulose Substances 0.000 description 1
- 235000010981 methylcellulose Nutrition 0.000 description 1
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 230000010355 oscillation Effects 0.000 description 1
- 229940055695 pancreatin Drugs 0.000 description 1
- 239000004584 polyacrylic acid Substances 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 229940071089 sarcosinate Drugs 0.000 description 1
- 210000002374 sebum Anatomy 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 229960000776 sodium tetradecyl sulfate Drugs 0.000 description 1
- DAJSVUQLFFJUSX-UHFFFAOYSA-M sodium;dodecane-1-sulfonate Chemical compound [Na+].CCCCCCCCCCCCS([O-])(=O)=O DAJSVUQLFFJUSX-UHFFFAOYSA-M 0.000 description 1
- AYFACLKQYVTXNS-UHFFFAOYSA-M sodium;tetradecane-1-sulfonate Chemical compound [Na+].CCCCCCCCCCCCCCS([O-])(=O)=O AYFACLKQYVTXNS-UHFFFAOYSA-M 0.000 description 1
- UPUIQOIQVMNQAP-UHFFFAOYSA-M sodium;tetradecyl sulfate Chemical compound [Na+].CCCCCCCCCCCCCCOS([O-])(=O)=O UPUIQOIQVMNQAP-UHFFFAOYSA-M 0.000 description 1
- 229940100515 sorbitan Drugs 0.000 description 1
- 229940035044 sorbitan monolaurate Drugs 0.000 description 1
- 235000011071 sorbitan monopalmitate Nutrition 0.000 description 1
- 239000001570 sorbitan monopalmitate Substances 0.000 description 1
- 229940031953 sorbitan monopalmitate Drugs 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 238000004506 ultrasonic cleaning Methods 0.000 description 1
Landscapes
- Eyeglasses (AREA)
- Detergent Compositions (AREA)
Abstract
Description
【発明の詳細な説明】
(産業上の利用分野)
本発明はコンタクトレンズ、眼内レンズ、眼鏡レンズの
医療内光学レンズ等の精密部品を洗浄する洗浄方法と洗
浄装置に関するものである。DETAILED DESCRIPTION OF THE INVENTION (Field of Industrial Application) The present invention relates to a cleaning method and a cleaning apparatus for cleaning precision parts such as contact lenses, intraocular lenses, and medical optical lenses such as eyeglass lenses.
(従来技術)
従来の医療用光学レンズ特に、コンタクトレンズの洗浄
は界面活性剤を主成分とする溶液での手指による洗浄や
溶液に超音波や熱を加える等の方法(特公昭53−16
629号)や、食塩水中に電流を流して次亜塩素酸塩を
作り、これにより消毒する方法(特公昭60−2055
号)、又は電解液をイオン交換膜を用いて酸、アルカリ
液に分離しアルカリ液と超音波にて洗浄する方法(特開
昭63−254417号)、更に又、蛋白分解酵素やイ
オン分解酵素を主成分とする通称エンザイム処理剤(特
開昭50−31834号、特開昭50−64303号、
特公昭5フー48712号)を利用する洗浄方法がある
。(Prior art) Conventional medical optical lenses, especially contact lenses, can be cleaned using methods such as washing by hand with a solution containing a surfactant as a main component or applying ultrasound or heat to the solution (Japanese Patent Publication No. 53-16
No. 629), and a method for disinfection by passing an electric current through saline water to create hypochlorite (Special Publication No. 60-2055).
(No. 63-254417), or a method in which the electrolyte is separated into acid and alkaline solutions using an ion exchange membrane and washed with the alkaline solution and ultrasonic waves (Japanese Patent Application Laid-Open No. 63-254417), and also proteolytic enzymes and ionolytic enzymes. Commonly known enzyme treatment agents containing as main ingredients (JP-A-50-31834, JP-A-50-64303,
There is a cleaning method that uses a special public service (Special Publication No. 5 Fu 48712).
(発明が解決しようとする課ml)
従来に於ける前述した如き、界面活性剤での手指の洗浄
ではその効果は薄く、又レンズ自体を傷付けたり破損す
ることが多かった、 又、超音波洗浄機を使用した場合
でもキャビテーションによる効果は見られるもののリゾ
チームを主とする蛋白質の除去には至らなかった、 加
えて電離を主眼とするものに於いてもリゾチーム層を遊
離せしむるに困難さが見られる、 一方、エンザイム処
理剤にあっては本来、液温を高める程、例えば室温略6
GC位がその活性には好ましいと言われているものの、
そのほとんどの使用が室温で行なわれ、十分に効力を発
し得ない、 又、上記の各方法に於いてその沈積物が溶
解除去されたとしてもその物質の再付着という点におい
ては何等考慮されていないのが現状である。(Problem to be solved by the invention) As mentioned above, conventional cleaning of hands and fingers with a surfactant has little effect and often damages or damages the lens itself.Also, ultrasonic cleaning Even when a machine was used, the effect of cavitation was seen, but it was not able to remove proteins mainly composed of lysozyme.In addition, even when the main focus was on ionization, it was difficult to release the lysozyme layer. On the other hand, with enzyme treatment agents, the higher the liquid temperature, for example, the room temperature
Although the GC position is said to be preferable for its activity,
Most of their uses are carried out at room temperature, so they are not fully effective, and even if the deposits are dissolved and removed in the above methods, no consideration is given to re-deposition of the substance. The current situation is that there is no such thing.
本発明は、上記問題点に基きレンズを傷めることなく速
やかに洗浄し、再付着による眼への悪影響を考慮して洗
浄効果を高める洗浄方法とその装置を提供するものであ
る。In view of the above-mentioned problems, the present invention provides a cleaning method and apparatus for cleaning the lens quickly without damaging it, and increasing the cleaning effect while taking into account the adverse effects on the eyes due to re-deposition.
(1題を解決するための手段)
上記問題点を解決する方法としては洗浄液の活性を最大
にする為に、洗浄液に通電することで上昇する液温を冷
却槽にて適温に保ち、洗浄液Cl−イオン、Na イオ
ンによって溶解遊離された被洗浄体の沈積物を超音波等
の物理的力にて増強された電気泳動力により親水性ゲル
又はコロイドゾル内に封止して沈積物の被洗浄体への再
付着を防ぐ洗浄方法とその装匠を提供するものである。(Means for Solving Problem 1) To solve the above problem, in order to maximize the activity of the cleaning liquid, the temperature of the cleaning liquid, which increases by energizing it, is kept at an appropriate temperature in a cooling tank, and the cleaning liquid Cl - The deposits of the object to be cleaned, dissolved and liberated by Na ions and Na ions, are sealed in a hydrophilic gel or colloidal sol by electrophoretic force enhanced by physical force such as ultrasonic waves, and the deposits are sealed in the object to be cleaned. The purpose of this invention is to provide a cleaning method that prevents re-adhesion to the surface and its decoration.
即ち、従来、光学レンズへの汚染物の沈稙については該
光学レンズの表面付近のマイナスチャージに依る場合が
多いと言われている、(第5図C参照)一般的な洗浄方
法である洗浄剤のみでの洗浄や酸アルカリ処理などもこ
の陽イオン化された沈積物の遊離に効果が見られるもの
の完全な状態にはまだ遠い。That is, conventionally, it has been said that the settling of contaminants on an optical lens is often due to negative charges near the surface of the optical lens (see Figure 5C), which is a common cleaning method. Although cleaning with only chemicals and acid-alkali treatment are effective in liberating the cationized deposits, they are still far from perfect.
そこで親水性ゲル又はコロイドゾル内に通電して生じる
電気泳動力を利用し遊離効果を上げる、(第5図す参照
) 然し、この遊離されたままの状態では通電を止めた
時や、洗浄剤の活性が死活した時には沈積物の再付着が
問題になる、(第5図C参照)而して、本発明の主点で
ある電気泳動により親水性ゲル又はコロイドゾル内に遊
離した沈積物を封止せしめて光学レンズ等への再付着を
防ぎ、洗浄効果を向上せしめるものである。Therefore, the electrophoretic force generated by applying electricity to the hydrophilic gel or colloidal sol is used to increase the release effect (see Figure 5). When the activity is dead, re-deposition of deposits becomes a problem (see Figure 5C).Thus, the main point of the present invention is to seal the liberated deposits in a hydrophilic gel or colloidal sol by electrophoresis. At the very least, it prevents re-adhesion to optical lenses and the like and improves the cleaning effect.
(作 用)
本発明は上記した方法によって医療用光学レンズの沈積
物を洗浄するものであるから、洗浄液による無機物、油
脂や眼脂、涙液成分、蛋白質を溶解する作用と洗浄槽間
を通電することにより発生するC見−イオン 、Na°
イオンによる酸、アルカリ処理での沈積物の除去作用、
通電による親水性ゲル又はコロイドゾル内に発生する電
気泳動力を物理的力によって増強して溶解除去した沈積
物を該親水性ゲル又はコロイドゾル内に泳動し貝止滞留
することにより溶解除去した沈積物の被洗浄体への再付
着を防いで効率の良い洗浄を完成することが出来る。(Function) Since the present invention cleans deposits on medical optical lenses by the above-described method, the cleaning solution dissolves inorganic substances, oils, eye sebum, tear fluid components, and proteins, and the current is passed between the cleaning tank. C-ion generated by , Na°
Removal of deposits through acid and alkali treatment with ions,
The electrophoretic force generated in a hydrophilic gel or colloidal sol by applying electricity is enhanced by physical force to dissolve and remove the sediment. It is possible to complete efficient cleaning by preventing re-adhesion to the object to be cleaned.
(実施例)
実施例について図面(第1図乃至第4図)を参照して説
明する。(Example) An example will be described with reference to the drawings (FIGS. 1 to 4).
m1図中、lは洗浄と電気泳動を行なう為のカートリ、
ジ本体であり、異種電極に対応して一対の洗浄槽(2A
、2B)を距離皇だけ隔離した状態にて底面部3を介
して連設せしめると共に、該底面部3内には電気泳動部
材Pとしての親水性ゲル又はコロイドゾルを左右均等に
充填せしめである。In the m1 diagram, l is a cartridge for washing and electrophoresis,
It has a pair of cleaning tanks (2A) corresponding to different types of electrodes.
, 2B) are connected to each other via the bottom part 3 while being separated by a distance, and the bottom part 3 is evenly filled with hydrophilic gel or colloidal sol as the electrophoretic member P on the left and right sides.
而して、前記一対の洗浄槽(2A 、2B)間に介在せ
しめた電気泳動部材Pに、該洗浄槽(2A 、 2B)
内に予め充填した洗浄液4(界面活性剤等)を介して外
部電極(5A、5B)により電圧を加えた際には、第3
図aに示す如く電気泳動部材Pとしての親水性ゲル又は
コロイドゾル中のイオン又はコロイド粒子が一方の極側
へ移動するために該夫々の洗浄槽(2A、2B)間には
底面部3を介して適宜電位差が発生することとなる。Thus, the cleaning tanks (2A, 2B) are attached to the electrophoretic member P interposed between the pair of cleaning tanks (2A, 2B).
When a voltage is applied by the external electrodes (5A, 5B) through the cleaning liquid 4 (surfactant, etc.) that has been filled in advance, the third
As shown in Figure a, in order for the ions or colloidal particles in the hydrophilic gel or colloidal sol as the electrophoretic member P to move to one pole side, there is a bottom part 3 between the respective cleaning tanks (2A, 2B). Therefore, an appropriate potential difference is generated.
前記した電気泳動部材Pとしての親水性ゲル又はコロイ
ドゾルにはポリアクリル酸アミド、メチルセルロース、
エチルセルロース、ヒドロキシエチルアクリレート、ヒ
ドロキシプロピルアクリレート、CMC,HEMA!′
gを使用し、又前記洗浄液4としてはラウリル硫酸ナト
リウム、ドデシル硫酸ナトリウム、ドデシルスルホン酸
ナトリウム、テトラデシル硫酸ナトリウム、テトラデシ
ルスルホン酸ナトリウム、ドデシルベンゼン、スルホン
酸ナトリウム、ドデシルNサルコシン酸ナトリウム、P
OE等の陰イオン界面活性剤、ポリエチレン、ポリプロ
ピレンエステル、デシルエーテル、ドデシルエーテル、
トリデシルエーテル、テトラデシルエーテル、セチルエ
ーテル、ステフリルエーテル、セチルステアクリルエー
テル、p−をオクチルフェニルエーテル、pオクチルフ
ェニルエーテル、モノラウリン酸ソルビタン、モノパル
ミチン酸ソルビタン、モノステアクリン酸ソルビタン等
の弊イオン界面活性剤及びトリプシン、パパイン、キモ
トリプシン、キモパパイン等の蛋白分解酵素、りバーゼ
、ジアスターゼ、パンクレアチン等の脂肪酸分解酵素、
アミラーゼ、トルドウス、グルコアミラーゼ等のムチン
分解酵素、キレート剤としてのEDTA (エチレンジ
アミン四酢酸)、NTA (ニトリロ三酢酸)、UDA
(ウラミルニ酢酸)、Ampho l i ne (
アコム社製)、コール酸、ディオキシコール酸等の肝汁
酸等を含み、侵透圧が略200乃至300の間に調整さ
れた水溶液を使用する。The hydrophilic gel or colloidal sol as the electrophoretic member P mentioned above includes polyacrylic acid amide, methyl cellulose,
Ethylcellulose, hydroxyethyl acrylate, hydroxypropyl acrylate, CMC, HEMA! ′
The washing liquid 4 includes sodium lauryl sulfate, sodium dodecyl sulfate, sodium dodecyl sulfonate, sodium tetradecyl sulfate, sodium tetradecyl sulfonate, dodecylbenzene, sodium sulfonate, sodium dodecyl N-sarcosinate, P
Anionic surfactants such as OE, polyethylene, polypropylene ester, decyl ether, dodecyl ether,
Our ionic interfaces include tridecyl ether, tetradecyl ether, cetyl ether, stefryl ether, cetyl stearyl ether, p-octylphenyl ether, p-octylphenyl ether, sorbitan monolaurate, sorbitan monopalmitate, sorbitan monostearacrate, etc. activators and proteolytic enzymes such as trypsin, papain, chymotrypsin, and chymopapain; fatty acid degrading enzymes such as libase, diastase, and pancreatin;
Mucin-degrading enzymes such as amylase, Trudous, and glucoamylase, EDTA (ethylenediaminetetraacetic acid), NTA (nitrilotriacetic acid), and UDA as chelating agents
(uramyl diacetic acid), Ampholine (
An aqueous solution containing liver juice acids such as Acom Co., Ltd.), cholic acid, dioxycholic acid, etc. and having an osmotic pressure adjusted to between about 200 and 300 is used.
然る時、電気泳動部材Pとしての親水性ゲル又はコロイ
ドゾル中の電子の流れは、第3図すに示す如く洗浄液4
の界面活性剤濃度の増加に伴い逆転せしめられ、正の界
面電気量が負極側へ蓄積される状態から負の界面電気量
が正極側へ蓄積される状態へ移行する、 6は洗浄装置
本体で、前記カートリッジ本体lを挿入する為のカート
リッジ挿入部7を形成しである、(第2図参照)
8はカートリッジ挿入部7の底部に形成した冷却槽であ
り、親水性ゲル又はコロイドゾルへの冷却と。At that time, the flow of electrons in the hydrophilic gel or colloidal sol as the electrophoretic member P is caused by the cleaning liquid 4 as shown in FIG.
6 is the cleaning device main body. , which forms a cartridge insertion part 7 for inserting the cartridge main body 1 (see Fig. 2). 8 is a cooling tank formed at the bottom of the cartridge insertion part 7, which cools the hydrophilic gel or colloidal sol. and.
後述する。tfl−g波伝導の作用を有する水Wが冷却
循環装置9のコントロールで水温水圧を一定に保持した
まま冷却槽8の注入一口8Aから注入され排出口8Bか
ら冷却循瑚装2t9へ環流すべく成しである。This will be explained later. Water W having the action of TFL-G wave conduction is injected from the inlet 8A of the cooling tank 8 while keeping the water temperature and water pressure constant under the control of the cooling circulation device 9, and is circulated from the discharge port 8B to the cooling circulation device 2t9. It is completed.
尚、@記冷却水の代りに炭酸ガス或いはアンモニアの注
入排出を利用しても良い。Incidentally, instead of the cooling water mentioned above, injection and discharge of carbon dioxide gas or ammonia may be used.
10は二本の接続端子用脚fit OA及びIOBと脚
部10C及び100とを右する上蓋であり、前記洗浄槽
(2A、2B)に夫々対向した位置には前記接続端子用
脚PJIOA、IOBと夫々導通した外部電極5A 、
5Bを垂下せしめである。Reference numeral 10 denotes an upper lid that holds two connection terminal legs fit OA and IOB and leg parts 10C and 100, and the connection terminal legs PJIOA and IOB are located at positions facing the cleaning tanks (2A, 2B), respectively. external electrodes 5A electrically connected to the external electrodes 5A,
5B is allowed to hang down.
11A及びIIBは洗浄装置本体6にセットされたカー
トリッジ本体lの洗浄槽(2A 、2B)内に被洗浄体
を投置するための導電メー、キされたプラスチック又は
炭素繊維等で成型された導電性を有する洗浄用網籠であ
り、該洗沙用網m(IIA、11B)に先ず被洗浄体を
入れた後、その上周縁に形成した取付凸部12Aを前記
外部電極(5A 、5B)の外周に形成した取付四部1
2Bに嵌合せしめることで取付が完了する、 然る時、
洗浄用銅fi(IIA。11A and IIB are conductive molds for placing objects to be cleaned into the cleaning tanks (2A, 2B) of the cartridge main body 1 set in the cleaning device main body 6, and conductive metal molded from hardened plastic or carbon fiber. After first putting the object to be cleaned into the washing net m (IIA, 11B), attaching the mounting protrusion 12A formed on the upper periphery to the external electrode (5A, 5B). Four mounting parts 1 formed on the outer periphery of
Installation is completed by fitting 2B.
Cleaning copper fi (IIA.
118)は外部電極(5A、5B)を介して前記接続端
子用脚部(IOA、10B)と夫々導通する。118) are electrically connected to the connection terminal legs (IOA, 10B) via external electrodes (5A, 5B), respectively.
14A、14B、14c、!40は前記洗浄装置本体6
の四周に穿った前記接続端子用脚部(10A。14A, 14B, 14c,! 40 is the cleaning device main body 6
The connection terminal legs (10A) are drilled around the four sides of the connection terminal.
108)及び脚部(l QC、l 00)を挿入するた
めの挿入孔であり、この内前記接続端子用脚部(IOA
、10B)に対向する処の該挿入孔14A及び14Bの
中には外部の電気制御装置i15に接続した入力端子1
6A及び16Bを埋設せしめである。108) and leg portions (l QC, l 00), of which the connection terminal leg portion (IOA
, 10B) are provided with input terminals 1 connected to an external electric control device i15 in the insertion holes 14A and 14B.
6A and 16B are buried.
而して、上蓋10を洗浄装置本体6に閉蓋密着した際に
は前記接続端子用脚i! (l OA−,l OB)と
入力端子(16A 、 16B)とが夫々接続して外部
の電気制御装W115と導通すべく成しである。Therefore, when the upper lid 10 is closed and tightly attached to the cleaning device main body 6, the connection terminal leg i! (l OA-, l OB) and input terminals (16A, 16B) are connected to each other so as to be electrically connected to the external electric control device W115.
17は超音波発振子であり前記冷却槽8下部に端子17
A及び17Bを介して取付けである。17 is an ultrasonic oscillator, and a terminal 17 is provided at the bottom of the cooling tank 8.
Attachment is through A and 17B.
又、該端子(17A 、 17B)は前記入力端子(1
6A、16B)とともに電気制御装置115へ接続しで
ある、 而して、該超音波発振子17は電気制御装2!
15のコントロール下でタイマーによる通電時間を可変
することが出来る。Further, the terminals (17A, 17B) are connected to the input terminal (1
6A, 16B) to the electric control device 115, and the ultrasonic oscillator 17 is connected to the electric control device 2!
The energization time can be varied by a timer under the control of 15.
然る時、前記冷却槽8内の水W及び底面部3内の電気泳
動部材Pを介して洗浄槽(2A、2B)内の洗浄液4側
へ超音波発振子17の超音波が伝導せしめられ、これに
より電気泳動部材P内に強制的に振動電位差(デバイ効
果)を励起せしめ、被洗浄体の沈積物を對止滞留するた
めの電気泳動力を増強せしめ得る。At this time, the ultrasonic waves of the ultrasonic oscillator 17 are transmitted to the cleaning liquid 4 side in the cleaning tanks (2A, 2B) via the water W in the cooling tank 8 and the electrophoretic member P in the bottom part 3. As a result, an oscillating potential difference (Debye effect) is forcibly excited in the electrophoretic member P, and the electrophoretic force for retaining deposits on the object to be cleaned can be enhanced.
次ぎに本発明の使用態様について説明する。Next, the mode of use of the present invention will be explained.
先ず、カセット本体lを洗浄装置本体6のカートリッジ
挿入部7内に収容し該カートリッジ本体1の洗浄#g(
2A、2B)内に洗浄液4を満たす。First, the cassette body l is accommodated in the cartridge insertion part 7 of the cleaning device body 6, and the cartridge body 1 is cleaned #g(
2A, 2B) with cleaning liquid 4.
次いで、洗浄用網ME(IIA、IIB)内に夫々被洗
浄体を入れてこれを上蓋10の外部電極(5A。Next, the objects to be cleaned are placed in the cleaning nets ME (IIA, IIB) and connected to the external electrodes (5A) of the upper lid 10.
5B)に夫々取付けた後、これを洗浄装置本体6に閉蓋
する、 然る時、被洗浄体は洗浄液4内に投置すると共
に前記接続端子用脚部(10A 、 10B)と入力端
子(16A 、 16B)とが接続して外部の電気−制
御装置115に導通して洗浄が開始される。5B), and then close the lid on the cleaning device main body 6. At that time, the object to be cleaned is placed in the cleaning liquid 4, and the connecting terminal legs (10A, 10B) and the input terminal ( 16A, 16B) are connected to the external electric control device 115, and cleaning is started.
然る際、カートリツジ本体lの底面部3内に充填された
電気泳動部材Pが沈積物を電気泳動せしめ、これを該電
気泳動部材P内に封入滞留するので沈積物の被洗浄体へ
の再付着を防止することが出来る。At this time, the electrophoretic member P filled in the bottom part 3 of the cartridge main body 1 electrophoreses the deposits, and the deposits are sealed and retained in the electrophoretic member P, so that the deposits are not returned to the object to be cleaned. Adhesion can be prevented.
(発明の効果)
而して、本発明は親水性ゲル又はコロイドゾルで作られ
た洗浄槽で洗浄剤での洗浄、Cl−イオンと、Na−イ
オンでの酸アルカリ処理で溶解された沈積物を超音波等
の物理的力で強化された電気泳動力で親水性ゲル又はコ
ロイドゾル内に月止することが出来るので以下の効果が
ある。(Effects of the Invention) Therefore, the present invention removes dissolved deposits by cleaning with a cleaning agent and acid-alkali treatment with Cl- ions and Na- ions in a cleaning tank made of a hydrophilic gel or colloidal sol. It can be fixed in a hydrophilic gel or colloidal sol by electrophoretic force reinforced by physical force such as ultrasound, resulting in the following effects.
(1)従来の洗浄方法では考慮されていなかった溶解し
た沈積物の再付着を電気泳動により親水性ゲル又はコロ
イドゾル内に封止して防ぐことが出来た。(1) Re-deposition of dissolved deposits, which was not considered in conventional cleaning methods, could be prevented by sealing them in a hydrophilic gel or colloidal sol by electrophoresis.
(2)従来の電気泳動に超音波に依る強制振動電位差を
附与することによりその泳動力を強化した。(2) The electrophoretic force of conventional electrophoresis was strengthened by imparting a forced oscillation potential difference using ultrasound.
(3)洗浄剤の活性を最大にする為に洗浄液温を最、
適温度に保つよう冷却装置によりコントロール出来る。(3) In order to maximize the activity of the cleaning agent, adjust the temperature of the cleaning solution to the maximum.
It can be controlled by a cooling device to maintain the appropriate temperature.
第1図は本発明のカートリッジ本体の全体斜視図。
第2図は洗浄装置本体の拡大一部縦断正面図、第3図a
は洗浄方法の概略を示す原理的説明図、第3図すは電気
泳動部材の電子の流れ態様を説明するグラフ図であり、
第4図は洗浄装置本体の分解斜視図。
第5図a乃至Cは被洗浄物の汚染態様を示す縦断側面図
である。FIG. 1 is an overall perspective view of the cartridge main body of the present invention. Figure 2 is an enlarged partial longitudinal sectional front view of the main body of the cleaning device, Figure 3a
3 is a principle explanatory diagram showing an outline of the cleaning method, and FIG. 3 is a graph diagram illustrating the flow mode of electrons in the electrophoretic member.
FIG. 4 is an exploded perspective view of the main body of the cleaning device. FIGS. 5A to 5C are longitudinal sectional side views showing the manner of contamination of the object to be cleaned.
Claims (1)
動部材Pを、異種電極に対応した一対の洗浄槽(2A、
2B)間に介在せしめることにより被洗浄体を電気泳動
を伴って洗浄することを特徴とする洗浄方法 (2)親水性ゲル又はコロイドゾルによって設けられた
洗浄液槽で洗浄液による被洗浄体の沈積物の除去に、液
槽間の通電によるCl^−イオン、Na^+イオンの酸
アルカリ処理による溶解を加えると同時に物理的力によ
り増強された電気泳動力にて沈積物を前記親水性ゲル又
はコロイドゾル内に封止し、被洗浄体への沈積物の再付
着を防ぎ、洗浄液と親水性ゲル又はコロイドゾルの温度
をコントロールすることを特徴とする請求項1記載の洗
浄方法 (3)被洗浄体がコンタクトレンズ、眼内レンズ、眼鏡
レンズ等の医療用光学レンズであることを特徴とする請
求項1方至2記載の洗浄方法 (4)洗浄液がラウリル硫酸ナトリウム等の陰イオン界
面活性剤やポリエチレン、ポリプロピレンエステル等の
非イオン界面活性剤及びトリプシン、パパイン、キモト
リプシン、キモパパイン等のタンパク分解酵素、リパー
ゼ、ジアスターゼ等の脂肪酸分解酵素やムチン分解酵素
、又キレート剤としてEDTAAmpholine、コ
ール酸、ディオキシコール酸などの肝汁酸を含み、浸透
圧が略300程度の水溶液であることを特徴とする請求
項1乃至3記載の洗浄方法(5)親水性ゲル又はコロイ
ドゾルをポリアクリル酸、アミドメチルセルロース、エ
チルセルロース、ヒドロキシエチルアクリレート、ヒド
ロキシプロピルアクリレート、CMC、HEMA等を利
用することを特徴とする請求項1乃至4記載の洗浄方法
(6)電気泳動を行なう際に発生するCl^−イオン、
Na^+イオンを利用し被洗浄体を酸処理及びアルカリ
処理することにより洗浄液による洗浄を強化することを
特徴とする請求項1乃至5記載の洗浄方法(7)電気泳
動を行なう際に発生する熱を洗浄剤の活性を最大にする
ことと、泳動力を高めるために、冷却装置を使用して温
度をコントロールすることを特徴とする請求項1乃至6
記載の洗浄方法 (8)電気泳動力の増強の物理的力として超音波により
、親水性ゲル又はコロイドゾル内に強制的に振動電位差
を生じせしめたことを特徴とする請求項1乃至7記載の
洗浄方法 (9)アルカリ液のPHが1乃至13であることを特徴
とする請求項1乃至8記載の洗浄方法 (10)異種電極に対応して一対の洗浄槽(2A、2B
)を距離lだけ隔離して底面部3を介して連設せしめる
と共に、該底面部3内に左右均等に電気泳動部材Pを充
填せしめて成るカートリッジ本体1であって、該カート
リッジ本体1を、洗浄液温をコントロールする冷却水槽
を有し、電気泳動部材Pの泳動力を高める超音波発振装
置を設けた洗浄装置本体6内に着脱自在に装着せしめる
一方、該洗浄装置本体6が被洗浄体を保持する網籠を装
着し得る機構と外部電極を有する洗浄装置上蓋とを有し
、上蓋脚部を洗浄装置本体挿入部に挿入することで通電
が可能なことを特徴とする洗浄装置 (11)被洗浄体を洗浄液中に投入する際に外部電極部
と連結せしめる構造を持った導電性の金属、貴金属又は
導電メッキされたプラスチック、炭素繊維等で作られた
網籠を利用することを特徴とする請求項10記載の洗浄
装置[Scope of Claims] (1) An electrophoretic member P made of a hydrophilic gel or a colloidal sol is cleaned in a pair of cleaning tanks (2A,
2B) A cleaning method characterized by cleaning the object to be cleaned with electrophoresis by interposing the object between the two. For removal, Cl^- ions and Na^+ ions are dissolved by acid-alkali treatment by applying electricity between the liquid tanks, and at the same time, the deposits are transferred into the hydrophilic gel or colloid sol using electrophoretic force enhanced by physical force. (3) The cleaning method according to claim 1, characterized in that the cleaning method comprises: sealing the object to be cleaned to prevent deposits from re-adhering to the object to be cleaned, and controlling the temperature of the cleaning liquid and the hydrophilic gel or colloidal sol. The cleaning method according to claims 1 or 2, wherein the cleaning liquid is an anionic surfactant such as sodium lauryl sulfate, polyethylene, or polypropylene. Nonionic surfactants such as esters, proteolytic enzymes such as trypsin, papain, chymotrypsin, and chymopapain, fatty acid degrading enzymes such as lipase and diastase, mucin degrading enzymes, and chelating agents such as EDTA Ampholine, cholic acid, and dioxycholic acid. (5) The cleaning method according to any one of claims 1 to 3, characterized in that the aqueous solution contains liver juice acid and has an osmotic pressure of about 300. The cleaning method according to claims 1 to 4, characterized in that acrylate, hydroxypropyl acrylate, CMC, HEMA, etc. are used (6) Cl^- ions generated during electrophoresis;
A cleaning method according to claims 1 to 5, characterized in that cleaning by the cleaning solution is strengthened by subjecting the object to be cleaned to acid treatment and alkali treatment using Na^+ ions (7) that occur during electrophoresis. Claims 1 to 6, characterized in that the temperature is controlled using a cooling device in order to maximize the activity of the detergent and increase the electrophoretic force.
The cleaning method (8) according to any one of claims 1 to 7, characterized in that an oscillating potential difference is forcibly generated in the hydrophilic gel or colloidal sol using ultrasound as a physical force to enhance the electrophoretic force. Method (9) The cleaning method according to Claims 1 to 8, characterized in that the pH of the alkaline solution is 1 to 13. (10) A pair of cleaning tanks (2A, 2B) corresponding to different types of electrodes are used.
) are separated by a distance l and are connected to each other via a bottom part 3, and the bottom part 3 is filled with an electrophoretic member P evenly on the left and right sides, the cartridge main body 1 having: The cleaning device main body 6 has a cooling water tank for controlling the temperature of the cleaning liquid and is equipped with an ultrasonic oscillator that increases the electrophoretic force of the electrophoretic member P. A cleaning device (11) characterized in that it has a mechanism for attaching a holding mesh basket and a cleaning device top lid having an external electrode, and can be energized by inserting the top lid legs into the cleaning device main body insertion part (11) It is characterized by the use of a mesh basket made of conductive metal, noble metal, conductive plated plastic, carbon fiber, etc., which has a structure that connects with the external electrode part when the object to be cleaned is placed in the cleaning solution. The cleaning device according to claim 10
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP28754989A JPH03148624A (en) | 1989-11-06 | 1989-11-06 | Method and device for washing |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP28754989A JPH03148624A (en) | 1989-11-06 | 1989-11-06 | Method and device for washing |
Publications (1)
Publication Number | Publication Date |
---|---|
JPH03148624A true JPH03148624A (en) | 1991-06-25 |
Family
ID=17718778
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP28754989A Pending JPH03148624A (en) | 1989-11-06 | 1989-11-06 | Method and device for washing |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPH03148624A (en) |
Cited By (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5368708A (en) * | 1991-12-02 | 1994-11-29 | Isoclear, Inc. | Lens decontamination system |
US5439572A (en) * | 1991-12-02 | 1995-08-08 | Isoclear, Inc. | Lens protective encasement packet |
WO2012031446A1 (en) * | 2010-09-07 | 2012-03-15 | 万定丽 | Contact lens cleaning apparatus |
CN105549226A (en) * | 2016-03-08 | 2016-05-04 | 李红 | Corneal contact lens cleaning device and cleaning method adopting same |
WO2020024882A1 (en) * | 2018-08-01 | 2020-02-06 | 苏州三个臭皮匠生物科技有限公司 | Contact lens restorer |
-
1989
- 1989-11-06 JP JP28754989A patent/JPH03148624A/en active Pending
Cited By (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5368708A (en) * | 1991-12-02 | 1994-11-29 | Isoclear, Inc. | Lens decontamination system |
US5439572A (en) * | 1991-12-02 | 1995-08-08 | Isoclear, Inc. | Lens protective encasement packet |
US5529678A (en) * | 1991-12-02 | 1996-06-25 | Isoclear, Inc. | Lens decontamination system |
WO2012031446A1 (en) * | 2010-09-07 | 2012-03-15 | 万定丽 | Contact lens cleaning apparatus |
CN105549226A (en) * | 2016-03-08 | 2016-05-04 | 李红 | Corneal contact lens cleaning device and cleaning method adopting same |
WO2020024882A1 (en) * | 2018-08-01 | 2020-02-06 | 苏州三个臭皮匠生物科技有限公司 | Contact lens restorer |
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