Linked Life Data

6374969

Source:http://linkedlifedata.com/resource/pubmed/id/6374969

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-7-2
pubmed:abstractText
The proteolytic activity of hemorrhagic proteinase IV isolated from timber rattlesnake (Crotalus horridus horridus) venom was resistant to inactivation by trypsin, pronase and the proteolytic IIt fraction isolated from timber rattlesnake venom. SDS-polyacrylamide gel electrophoresis of the hemorrhagin incubated alone and with the three proteinases revealed that the addition of trypsin or the IIt fraction caused little apparent degradation of the hemorrhagin, whether or not the samples were reduced prior to electrophoresis. SDS electrophoresis of the hemorrhagin after incubation with pronase revealed a single band of 28,000 apparent molecular weight (as compared to 52,000 for the original hemorrhagin) if the samples were not reduced prior to electrophoresis, and a single band of 17,000 if reduced. If the hemorrhagin was reduced and alkylated, it was much more susceptible to hydrolysis by all three proteinases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
235-41
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Resistance of a hemorrhagic proteinase from timber rattlesnake venom to proteolytic degradation.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.