Document Detail


Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin.
MedLine Citation:
PMID:  2745407     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The hemorrhagic toxin Ht-d from venom of the Western diamondback rattlesnake is a metalloproteinase with a molecular weight of 23,234. Peptides were obtained from enzymatic and chemical digestions, separated by reverse-phase chromatography, and sequenced in a gas-phase sequenator. The sequence showed a putative zinc binding site similar to that of thermolysin and other metalloproteinases but no overall significant similarity to the sequences of other metalloproteinases and may represent a new subfamily of metalloproteinases. Ht-d was shown to degrade type IV collagen and gelatin types I, III, and V but not interstitial collagens. The digestion of type IV collagen and other basement membrane proteins may allow this proteinase to disrupt capillary membranes causing hemorrhage in surrounding tissues.
Authors:
J D Shannon; E N Baramova; J B Bjarnason; J W Fox
Related Documents :
10551857 - Molecular cloning and ultrastructural localization of the core protein of an eggshell m...
9372017 - Multimerin.
24465507 - Cell morphogenesis proteins are translationally controlled through utrs by the ndr/lats...
21907147 - Mutations in mtfmt underlie a human disorder of formylation causing impaired mitochondr...
1400467 - Cloning and characterization of a cysteine proteinase from saccharomyces cerevisiae.
18072207 - Role of group a streptococcus htra in the maturation of speb protease.
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  264     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1989 Jul 
Date Detail:
Created Date:  1989-08-14     Completed Date:  1989-08-14     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  11575-83     Citation Subset:  IM    
Affiliation:
Department of Microbiology, School of Medicine, University of Virginia, Charlottesville 22908.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acids / analysis*
Animals
Binding Sites
Chromatography, High Pressure Liquid
Collagen / metabolism*
Crotalid Venoms / metabolism*
Electrophoresis, Polyacrylamide Gel
Gelatin / metabolism*
Hydrolysis
Metalloendopeptidases / antagonists & inhibitors,  metabolism*
Molecular Sequence Data
Rats
Substrate Specificity
Zinc / metabolism
Grant Support
ID/Acronym/Agency:
GM31289/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Crotalid Venoms; 7440-66-6/Zinc; 9000-70-8/Gelatin; 9007-34-5/Collagen; EC 3.4.24.-/Metalloendopeptidases; EC 3.4.24.1/atrolysin A

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Ligand-induced modulation of the hepatic receptor for asialoglycoproteins. Evidence for the role of ...
Next Document:  The magnetic and electronic properties of Methanobacterium thermoautotrophicum (strain delta H) meth...