Linked Life Data

986184

Source:http://linkedlifedata.com/resource/pubmed/id/986184

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1976-11-1
pubmed:abstractText
The interaction of components of the prothrombinase complex, i.e. bovine Factor X or Factor Xa, bovine Factor V or Factor Va, phospholipid, and Ca2+, in various combinations was studied primarily by a gel filtration technique. In experiments, in which phospholipids ranging from those isolated from naturally occurring sources to those long chain (18 : 1) as well as short chain 6 : 0 and 7 : 0 fatty acids prepared by chemical and enzymatic synthesis were used, it was evident that a net negative surface charge on the lipid dispersions was one of the important requirements for interaction. Though the short chain fatty acid phospholipids interacted with the proteins of the prothrombinase complex, there was invariably a diminution in the activity of the enzyme complex. It was established that Factor V or Va did not bind Ca2+ and that the binding of either of these factors with phospholipids (with a net negative charge) was not dependent on Ca2+. However, the interaction of Factor X or Factor Xa with phospholipids with a negative charge required Ca2+. It was shown that Factor X could bind to the same type of lipid of lipid surface as that noted for Factor Xa. Of interest was the apparent difference in the phospholipid binding characteristics of the two variant forms of bovine plasma Factor X, i.e. X1 and X2, which might in part explain the differences in their specific activities. Of importance was the lack of demonstrable complex formation between Factors II, X and V in the absence of phospholipids and/or in the presence or absence of Ca2+. The significance of these results as they might apply to the configuration of the prothrombinase complex and its interaction with prothrombin plus the usefulness of the short chain fatty acid phospholipid in exploring these lipid-protein interactions are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
444
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
131-46
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Interactions of the components of the prothrombinase complex.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.