Linked Life Data

3629624

Source:http://linkedlifedata.com/resource/pubmed/id/3629624

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1987-10-8
pubmed:abstractText
Analysis of the binding of tributyltin chloride (TBT) to human erythrocyte membrane indicated a single class of binding site with an affinity of approximately 6.78 X 10(3) M-1, whereas dibutyltin dichloride (DBT) showed the presence of more than one class of binding sites with a high affinity value of 2.53 X 10(4) M-1 and a low affinity value of 2.06 X 10(3) M-1. Membrane protein binding studies revealed that both di- and tributyltin compounds bind significantly with band 3 protein of the erythrocyte membrane. These results indicate the significant interactions of erythrocyte membrane components with alkyltin compounds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0378-4274
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Interaction of di- and tributyltin chloride with human erythrocyte membrane.
pubmed:publicationType
Journal Article, In Vitro