Lindqvist et al., 1977 - Google Patents
Origin of esterases in human whole salivaLindqvist et al., 1977
- Document ID
- 1107765984914534685
- Author
- Lindqvist L
- Nord C
- Söder P
- Publication year
- Publication venue
- Enzyme
External Links
Snippet
Whole saliva of 59 healthy persons was used for determination of esterase activity. The pattern of esterase was studied by means of isoelectrofocusing on thin-layer acrylamide gels. The esterases found in whole saliva are suggested to be derived from the cells of the …
- 210000003296 Saliva 0 title abstract description 15
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)
- C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
-
- 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)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
-
- 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)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/02—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving viable micro-organisms
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Grenier et al. | Characterization of sodium dodecyl sulfate-stable Bacteroides gingivalis proteases by polyacrylamide gel electrophoresis | |
Lindqvist et al. | Origin of esterases in human whole saliva | |
Uitto et al. | A protease of Bacteroides gingivalis degrades cell surface and matrix glycoproteins of cultured gingival fibroblasts and induces secretion of collagenase and plasminogen activator | |
Uitto et al. | Isolation of a chymotrypsinlike enzyme from Treponema denticola | |
Trimble et al. | The use of endo-β-N-acetylglucosaminidase H in characterizing the structure and function of glycoproteins | |
Hearing et al. | Mammalian tyrosinase. Structural and functional interrelationship of isozymes | |
Inui et al. | The gene coding for a sphingolipid activator protein, SAP-1, is on human chromosome 10 | |
Sapolsky et al. | Multiple forms of cathepsin D from bovine uterus | |
Fujimura et al. | Purification and properties of a bacteriocin-like substance (acnecin) of oral Propionibacterium acnes | |
Möllby et al. | Biological activities contaminating preparations of phospholipase C (α-toxin) from Clostridium perfringens | |
Aoki et al. | Differences of frequency distributions of plasminogen phenotypes between Japanese and American populations: new methods for the detection of plasminogen variants | |
Jackson et al. | Identification and analysis of a collagenolytic activity in Streptococcus mutans | |
Germaine et al. | Proteolytic activity of Candida albicans: action on human salivary proteins | |
Fujimura et al. | Comparative properties of envelope-associated arginine-gingipains and lysine-gingipain of Porphyromonas gingivalis | |
Lindqvist et al. | Esterases in human saliva | |
Beutler et al. | Hybridization of glucose-6-phosphate dehydrogenase from rat and human erythrocytes | |
Higerd et al. | New method for obtaining IgA-specific protease | |
Söder et al. | Proteolytic activity of dental plaque material. I. Action of dental plaque material on azocoll, casein and gelatin | |
Wicher et al. | Interactions of Bacillus subtilis alkaline proteinases with α2-macroglobulin and α1-antitrypsin | |
Kortt et al. | Activities and partial purification of extracellular proteases of Bacteroides nodosus from virulent and benign footrot | |
Rajasingham et al. | A comparative study of the isoenzymes of mammalian a-amylase | |
Toshikazu et al. | Kasahara-variant alkaline phosphatase in a renal cell carcinoma | |
Kottel et al. | Differential release of membrane-bound alkaline phosphatase isoenzymes from tumor cells by bromelain | |
Masters et al. | Phylogenetic relationships among the Galaginae as indicated by erythrocytic allozymes | |
Allaker et al. | Production of hydrolytic enzymes by oral isolates of Eikenella corrodens |