Luong et al., 1988 - Google Patents
Synthesis and characterization of a water‐soluble affinity polymer for trypsin purificationLuong et al., 1988
- Document ID
- 9123939685159999000
- Author
- Luong J
- Male K
- Nguyen A
- Publication year
- Publication venue
- Biotechnology and bioengineering
External Links
Snippet
A specific ligand bound polymer has been synthesized for the purpose of purification and stabilization of trypsin, an easily autodigestible enzyme. The affinity polymer was formed by copolymerizing N‐acryloyl‐m‐aminobenzamidine, a strong trypsin inhibitor, and acrylamide …
- 108090000631 Trypsin 0 title abstract description 72
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6427—Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/8146—Metalloprotease (E.C. 3.4.24) inhibitors, e.g. tissue inhibitor of metallo proteinase, TIMP
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Luong et al. | Synthesis and characterization of a water‐soluble affinity polymer for trypsin purification | |
Hixson Jr et al. | Affinity chromatograpy: Purification of bovine trypsin and thrombin | |
Murphy et al. | Partial purification of collagenase and gelatinase from human polymorphonuclear leucocytes. Analysis of their actions on soluble and insoluble collagens | |
Cuatrecasas et al. | Selective enzyme purification by affinity chromatography. | |
Buttle et al. | Affinity purification of the novel cysteine proteinase papaya proteinase IV, and papain from papaya latex | |
Rigbi et al. | Limited proteolysis of the bovine pancreatic secretory trypsin inhibitor at acid pH | |
Sim et al. | [5] Preparation and properties of human C1 inhibitor | |
Misono et al. | Characterization of the active site of mouse submaxillary gland renin | |
Feinstein | Purification of trypsin by affinity chromatography on ovomucoid‐sepharose resin | |
Sears et al. | Comparison of soluble and immobilized trypsin kinetics: Implications for peptide synthesis | |
Male et al. | Studies on the application of a newly synthesized polymer for trypsin purification | |
Male et al. | Isolation of urokinase by affinity ultrafiltration | |
Mornet et al. | Involvement of an arginyl residue in the catalytic activity of myosin heads | |
Oliveira et al. | Tyrosine 151 is part of the substrate activation binding site of bovine trypsin. Identification by covalent labeling with p-diazoniumbenzamidine and kinetic characterization of Tyr-151-(p-benzamidino)-azo-beta-trypsin. | |
Pesciotta et al. | Purification and characterization of the amino-terminal propeptide of pro. alpha. 1 (I) chains from embryonic chick tendon procollagen | |
Steers Jr et al. | [34] β-Galactosidase | |
Brown et al. | Sensitive fluorescent determination of trypsin-like proteases | |
US4973554A (en) | Affinity process for trypsin purification and stabilization | |
Uren | Affinity chromatography of proteolytic enzymes | |
Plummer Jr | Evidence for a carboxyl group at the active center of bovine carboxypeptidase B | |
Gleisner et al. | The structure of dihydrofolate reductase. I. Inactivation of bacterial dihydrofolate reductase concomitant with modification of a methionine residue at the active site. | |
SU644796A1 (en) | Method of purifying proteolytic ferments | |
Iwasaki et al. | Identification of the reactive site of potato proteinase inhibitor II-b for bovine chymotrypsin and a bacterial proteinase | |
Keilova et al. | Inhibition of cathepsin E by diazoacetyl-norleucine methyl ester | |
Eddy et al. | Chymotrypsin inhibitor from potatoes: interaction with target enzymes |