Nothing Special   »   [go: up one dir, main page]

Hovinga et al., 1994 - Google Patents

Coagulation factor XII Locarno: the functional defect is caused by the amino acid substitution Arg 353--> Pro leading to loss of a kallikrein cleavage site

Hovinga et al., 1994

View HTML
Document ID
13227121078607315482
Author
Hovinga J
Schaller J
Stricker H
Wuillemin W
Furlan M
Lammle B
Publication year

External Links

Snippet

The dysfunctional coagulation factor XII (FXII) Locarno was purified from 2 L of the proposita's plasma. Studies to identify the molecular defect responsible for the lack of amidolytic and proteolytic activity of this FXII variant were performed. Amino acid sequence …
Continue reading at www.sciencedirect.com (HTML) (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)
    • 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
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/745—Blood coagulation or fibrinolysis factors
    • C07K14/75—Fibrinogen
    • 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
    • A61K38/55—Protease inhibitors
    • A61K38/57—Protease inhibitors from animals; from humans
    • 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)

Similar Documents

Publication Publication Date Title
Hovinga et al. Coagulation factor XII Locarno: the functional defect is caused by the amino acid substitution Arg 353--> Pro leading to loss of a kallikrein cleavage site
Kisiel et al. Anticoagulant properties of bovine plasma protein C following activation by thrombin
Olson et al. Regulation of thrombin activity by antithrombin and heparin
Citarella et al. Structure/function analysis of human factor XII using recombinant deletion mutants: evidence for an additional region involved in the binding to negatively charged surfaces
Thaler et al. A simple two‐step isolation procedure for human and bovine antithrombin II/III (heparin cofactor): a comparison of two methods
Wesselschmidt et al. Tissue factor pathway inhibitor: the carboxy-terminus is required for optimal inhibition of factor Xa
Kisiel et al. Characterization of a protein C activator from Agkistrodon contortrix contortrix venom.
Dahlbäck et al. Localization of thrombin cleavage sites in the amino-terminal region of bovine protein S.
US20040033566A1 (en) Modified factor viia
Wu et al. The cleavage and inactivation of plasminogen activator inhibitor type 1 by neutrophil elastase: the evaluation of its physiologic relevance in fibrinolysis
Reber et al. Three abnormal fibrinogen variants with the same amino acid substitution (γ 275 Arg→ His): Fibrinogens Bergamo II, Essen and Perugia
US5770699A (en) Process for production of inhibited forms of activated blood factors
Patston et al. Reactivity of alpha 1-antitrypsin mutants against proteolytic enzymes of the kallikrein-kinin, complement, and fibrinolytic systems.
Apitz-Castro et al. Purification and partial characterization of draculin, the anticoagulant factor present in the saliva of vampire bats (Desmodus rotundus)
Olson et al. Role of protein conformational changes, surface approximation and protein cofactors in heparin-accelerated antithrombin-proteinase reactions
US8741844B2 (en) Use of mutated antithrombins for treating or preventing coagulation disorders
US20090298779A1 (en) Peptides which Modulate Blood Coagulation and Methods of Use Thereof
Erdjument et al. Antithrombin Milano, single amino acid substitution at the reactive site, Arg393 to Cys
Stone et al. Hirudin interactions with thrombin
Samis et al. Neutrophil elastase cleavage of human factor IX generates an activated factor IX-like product devoid of coagulant function
Citarella et al. Control of human coagulation by recombinant serine proteases: Blood clotting is activated by recombinant factor XII deleted of five regulatory domains
US5510248A (en) Stable recombinant meizothrombin-like polypeptides
Carter et al. Cabbage seed protease inhibitor: a slow, tight-binding inhibitor of trypsin with activity toward thrombin, activated Stuart factor (factor Xa), activated Hageman factor (factor XIIa), and plasmin
US20040110688A1 (en) Region of factor IXa protease domain that interacts with factor VIIIa and methods therefor
EP0239644A1 (en) Novel physiologically active substance having blood coagulation controlling activity