Linked Life Data

11024495

Source:http://linkedlifedata.com/resource/pubmed/id/11024495

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-11-30
pubmed:abstractText
A thrombin-like enzyme and a fibrinolytic serine protease were purified to homogeneity from the venom of a Korean snake Agkistrodon saxatilis emelianov. Both the purified enzymes migrated as a single protein band corresponding to 39 kDa in SDS-PAGE. However, the molecular mass was reduced to 28 kDa by enzymatic removal of the N-linked carbohydrates in those two different enzyme species. Although the thrombin-like enzyme and the fibrinolytic protease show homologous features in their molecular sizes and N-terminal amino acid sequences, yet they can be clearly distinguished from each other in terms of substrate specificity, susceptibility to inhibitors and fibrinogen degradation. It is postulated that these two enzymes are capable of functioning in a cooperative manner to effectively remove fibrinogen and consequently to reduce the blood viscosity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
555-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Biochemical characterization of a thrombin-like enzyme and a fibrinolytic serine protease from snake (Agkistrodon saxatilis) venom.
pubmed:affiliation
Department of Biochemistry, College of Science and Bioproducts Research Center, Yonsei University, Seoul, South Korea.
pubmed:publicationType
Journal Article