[go: up one dir, main page]

Okamoto et al., 1980 - Google Patents

A new polypeptide substrate, Suc-Tyr-Leu-Val-pNA, specific for spleen fibrinolytic proteinase (SFP)

Okamoto et al., 1980

Document ID
9529810204900655967
Author
Okamoto U
Nagamatsu Y
Tsuda Y
Okada Y
Publication year
Publication venue
Biochemical and Biophysical Research Communications

External Links

Snippet

In a search for an adequate synthetic substrate for human spleen fibrinolytic proteinase (SFP), Suc-Tyr-Leu-Val-pNA was newly synthesized. Its degradation by SFP was compared with that of other synthetic polypeptide substrates. Suc-Tyr-Leu-Val-pNA was degraded by …
Continue reading at www.sciencedirect.com (other versions)

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
    • 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)
    • C12N9/6456—Plasminogen activators
    • 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
    • C12N9/54—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria bacteria being Bacillus
    • 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)
    • C12Y304/21—Serine endopeptidases (3.4.21)
    • C12Y304/21069—Protein C activated (3.4.21.69)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/06—Dipeptides
    • C07K5/06086—Dipeptides with the first amino acid being basic
    • C07K5/06095—Arg-amino acid
    • 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
    • C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
    • C07K14/8121—Serpins

Similar Documents

Publication Publication Date Title
Graf et al. Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin
Odake et al. Human and murine cytotoxic T lymphocyte serine proteases: subsite mapping with peptide thioester substrates and inhibition of enzyme activity and cytolysis by isocoumarins
SUZUKI et al. Mechanism of inhibition of activated protein C by protein C inhibitor
US4318904A (en) Peptide affinity labels for thrombin and other trypsin-like proteases
US5147790A (en) Serum-independent human cell lines, process for producing same, and processes for producing proteins therefrom
Ohno et al. FOY:[Ethylp-(6-guanidinohexanoyloxy) benzoate] methanesulfonate as a serine proteinase inhibitor. I. Inhibition of thrombin and factor Xa in vitro
AU623769B2 (en) Proteinase inhibitors, process for the preparation thereof and medicaments containing these
SASAKI et al. Inactivation of calpain I and calpain II by specificity-oriented tripeptidyl chloromethyl ketones
Okamoto et al. A new polypeptide substrate, Suc-Tyr-Leu-Val-pNA, specific for spleen fibrinolytic proteinase (SFP)
Morihara et al. Subtilisin BPN′: Inactivation by chloromethyl ketone derivatives of peptide substrates
Largman Isolation and characterization of rat pancreatic elastase
Rhee et al. Role of meizothrombin and meizothrombin-(des F1) in the conversion of prothrombin to thrombin by the Echis carinatus venom coagulant
BASAK et al. Design and synthesis of novel inhibitors of prohormone convertases
Morihara et al. On the specificity of Bacillus subtilis neutral protease in relation to the compound active site
Wakselman et al. New mechanism-based inactivators of trypsin-like proteinases. Selective inactivation of urokinase by functionalized cyclopeptides incorporating a sulfoniomethyl-substituted m-aminobenzoic acid residue
Okada et al. Convenient purification of human spleen fibrinolytic proteinase (SFP) and human leucocyte elastase by affinity chromatography
Powers et al. [1] Peptide thioester substrates for serine peptidases and metalloendopeptidases
Pohl et al. Differences between uterine and melanoma forms of tissue plasminogen activator
US4892826A (en) Process for the preparation of urokinase derivatives
US5260060A (en) Fibrinolytic enzymes
TSUDA et al. Synthesis of tripeptide chloromethyl ketones and examination of their inhibitory effects on plasmin and plasma kallikrein
TSUDA et al. Synthesis of peptide chloromethyl ketones and examination of their inhibitory effects on human spleen fibrinolytic proteinase (SFP) and human leukocyte elastase (LE)
HU185454B (en) Process for seperating endoprotinase-lys-c
Lalmanach et al. Conserved cystatin segments as models for designing specific substrates and inhibitors of cysteine proteinases
OKADA et al. Synthesis of substrates specific for human spleen fibrinolytic proteinase (SFP)