Linked Life Data

2728027

Source:http://linkedlifedata.com/resource/pubmed/id/2728027

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-7-5
pubmed:abstractText
Protein fractionation techniques utilizing the different properties of the sample (size, charge, sugar moiety) were employed to characterize the crude A. c. contortrix venom. Gel filtration chromatography resolved about six to eight peaks, high performance liquid ion exchange chromatography and chromatofocusing about 12-14 peaks exhibiting hydrolytic activity. Two fibrin clot-promoting enzymes--both releasing fibrinopeptides A and fibrinopeptides B, but with different fibrinopeptide A/fibrinopeptide B relative rates were observed. The two enzymes (or enzyme isoforms) were serine proteinases with essentially the same hydrolytic activity towards low molecular chromogenic substrate for thrombin. They were of approximately the same size (one peak of 68,000 relative mol.wt on gel filtration chromatography), had apparent isoelectric points of about 6.4 and 5.4, respectively, and were glycoproteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
359-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Fibrinopeptide-releasing enzymes in the venom from the southern copperhead snake (Agkistrodon contortrix contortrix).
pubmed:affiliation
Institute of Hematology and Blood Transfusion, Prague, Czechoslovakia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't