Linked Life Data

7032585

Source:http://linkedlifedata.com/resource/pubmed/id/7032585

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1982-3-13
pubmed:abstractText
The proteolytic specificity of hemorrhagic toxin a from the venom of Crotalus atrox (western diamondback rattlesnake) has been investigated by using the oxidized B chain of bovine insulin and other peptides as substrates. The toxin appears highly specific for X--Leu bonds (cleaving the His10--Leu11, Ala14--Leu15, and Tyr16--Leu17 bonds), with no detectable activity against the Gly--Phe, Phe--Phe, Phe--Tyr, and Leu--Tyr bonds also present in the insulin B chain. The X--Leu bond of the peptides Tyr-Gly-Gly-Phe-Leu, Phe-Ala-Leu, and Ala-Leu was also cleaved. The toxin seems to be a strict endopeptidase, in that the cleavage of the two most susceptible bonds, Ala14--Leu15 and Tyr16--Leu17, are mutually exclusive; i.e., cleavage of either bond results in the other being too close to either the amino- or carboxyl-terminal of its respective fragment for the enzyme to be effective against it. The X--Met bond of Tyr-Gly-Gly-Phe-Met was cleaved, although a dipeptide Gly-Met was not hydrolyzed after 16 h of incubation. The substrates not hydrolyzed are furylacryloylglycyl-L-leucinamide, carbobenzoxy-L-glutamylglycine, carbobenzoxyglycyl-L-glutamic acid, benzoyl-L-arginine-p-nitroanilide, L-lysine-p-nitroanilide, (L-Ala)3-p-nitroanilide, Gly-Met, Gly-Phe-Phe, Gly-Gly-Ala, TAME, and ATEE. The absence of hydrolytic activity against the last two substrates indicates that hemorrhagic toxin a does not possess trypsin- or chymotrypsin-like activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7004-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Proteolytic specificity of hemorrhage toxin a isolated from western diamondback rattlesnake (Crotalus atrox) venom.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.