Linked Life Data

2480440

Source:http://linkedlifedata.com/resource/pubmed/id/2480440

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1990-1-25
pubmed:abstractText
Interaction of fractionated 3H-heparin with plasma proteins was investigated by gel filtration chromatography. The peak of the elution profile for fractionated 3H-heparin in rat plasma was observed at the higher molecular weight fraction than that for fractionated 3H-heparin in buffer without any protein, suggesting the existence of fractionated 3H-heparin binding protein(s) in plasma. Then the interaction of fractionated 3H-heparin with such plasma proteins as albumin, antithrombin III, thrombin and alpha-globulin was investigated. The elution profile for fractionated 3H-heparin in albumin solution, antithrombin III solution and the solution containing antithrombin III and thrombin were different from that for fractionated 3H-heparin in plasma. The elution profile for fractionated 3H-heparin in alpha-globulin solution, of a concentration close to that in plasma, was comparable to that of fractionated 3H-heparin in plasma, though two peaks were found. The major peak corresponded to that of fractionated 3H-heparin in plasma, and the minor peak eluted at a higher molecular weight fraction. When alpha-globulin concentration was decreased, the major peak shifted to the lower molecular weight fraction, and the minor peak was diminished and then disappeared. Thus it was suggested that alpha-globulin is dominant for plasma protein binding of fractionated 3H-heparin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0386-846X
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
416-22
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Investigation on interaction of fractionated 3H-heparin with plasma proteins by gel filtration chromatography.
pubmed:affiliation
Department of Biopharmaceutics, Faculty of Pharmaceutical Sciences, Nagoya City University, Japan.
pubmed:publicationType
Journal Article