[go: up one dir, main page]

Yee et al., 2018 - Google Patents

Inhibitors from Myanmar Russell's Viper Venom

Yee et al., 2018

View HTML
Document ID
5013182710900044297
Author
Yee K
Pitts M
Tongyoo P
Rojnuckarin P
Publication year
Publication venue
Snake Venom Metalloproteinases

External Links

Snippet

Russell's viper bites are potentially fatal from severe bleeding, renal failure and capillary leakage. Snake venom metalloproteinases (SVMPs) are attributed to these effects. In addition to specific antivenom therapy, endogenous inhibitors from snakes are of interest in …
Continue reading at books.google.com (HTML) (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424Serine endopeptidases (3.4.21)
    • C12N9/6427Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6402Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81Protease inhibitors
    • C07K14/8107Endopeptidase (E.C. 3.4.21-99) inhibitors
    • C07K14/8146Metalloprotease (E.C. 3.4.24) inhibitors, e.g. tissue inhibitor of metallo proteinase, TIMP
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/16Hydrolases (3) acting on ester bonds (3.1)
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81Protease inhibitors
    • C07K14/8107Endopeptidase (E.C. 3.4.21-99) inhibitors
    • C07K14/811Serine protease (E.C. 3.4.21) inhibitors
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00Medicinal preparations containing peptides
    • A61K38/16Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/43Enzymes; Proenzymes; Derivatives thereof
    • A61K38/46Hydrolases (3)
    • A61K38/48Hydrolases (3) acting on peptide bonds (3.4)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y304/00Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21Serine endopeptidases (3.4.21)

Similar Documents

Publication Publication Date Title
Kato et al. Changes in prolyl endopeptidase during maturation of rat brain and hydrolysis of substance P by the purified enzyme
Rao et al. Pseutarin C, a prothrombin activator from Pseudonaja textilis venom: its structural and functional similarity to mammalian coagulation factor Xa-Va complex
Rodrigues et al. Structural and functional characterization of neuwiedase, a nonhemorrhagic fibrin (ogen) olytic metalloprotease from Bothrops neuwiedi snake venom
Christiansen et al. Effect of fibroblast activation protein and α2-antiplasmin cleaving enzyme on collagen types I, III, and IV
López-Lozano et al. Ontogenetic variation of metalloproteinases and plasma coagulant activity in venoms of wild Bothrops atrox specimens from Amazonian rain forest
Franza Jr et al. Activation of human prothrombin by a procoagulant fraction from the venom of Echis carinatus. Identification of a high molecular weight intermediate with thrombin activity.
Bernardes et al. Proteomic analysis of Bothrops pirajai snake venom and characterization of BpirMP, a new PI metalloproteinase
Siigur et al. Biochemical characterization of lebetase, a direct-acting fibrinolytic enzyme from Vipera lebetina snake venom
Moradian‐Oldak et al. Controlled proteolysis of amelogenins reveals exposure of both carboxy‐and amino‐terminal regions
YU8997A (en) Purified protein having serinic proteaze inhibiting activity and pharmaceutical preparation containing them
Sanchez et al. A novel fibrinolytic metalloproteinase, barnettlysin-I from Bothrops barnetti (Barnett s pitviper) snake venom with anti-platelet properties
Sartim et al. Moojenactivase, a novel pro-coagulant PIIId metalloprotease isolated from Bothrops moojeni snake venom, activates coagulation factors II and X and induces tissue factor up-regulation in leukocytes
Pidde-Queiroz et al. PI snake venom metalloproteinase is able to activate the complement system by direct cleavage of central components of the cascade
Smolka et al. Purification and partial characterization of a thrombin-like enzyme, balterobin, from the venom of Bothrops alternatus
Sant'Ana et al. BjussuSP-I: a new thrombin-like enzyme isolated from Bothrops jararacussu snake venom
Sajevic et al. VaH3, one of the principal hemorrhagins in Vipera ammodytes ammodytes venom, is a homodimeric P-IIIc metalloproteinase
Sanz et al. Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries: insight into the evolution of the snake venom integrin-inhibition system
Leonardi et al. Hemorrhagin VaH4, a covalent heterodimeric P-III metalloproteinase from Vipera ammodytes ammodytes with a potential antitumour activity
de Albuquerque Modesto et al. Insularinase A, a prothrombin activator from Bothrops insularis venom, is a metalloprotease derived from a gene encoding protease and disintegrin domains
Kurtović et al. Ammodytagin, a heterodimeric metalloproteinase from Vipera ammodytes ammodytes venom with strong hemorrhagic activity
de Oliveira et al. Biochemical and functional characterization of BmooSP, a new serine protease from Bothrops moojeni snake venom
Gao et al. A novel prothrombin activator from the venom of Micropechis ikaheka: isolation and characterization
Boukhalfa-Abib et al. CcMP-II, a new hemorrhagic metalloproteinase from Cerastes cerastes snake venom: purification, biochemical characterization and amino acid sequence analysis
Leonardi et al. Two coagulation factor X activators from Vipera a. ammodytes venom with potential to treat patients with dysfunctional factors IXa or VIIa
Torres et al. Bmoo FIBMP‐I: A New Fibrinogenolytic Metalloproteinase from Bothrops moojeni Snake Venom