Linked Life Data

6127177

Source:http://linkedlifedata.com/resource/pubmed/id/6127177

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-12-16
pubmed:abstractText
High molecular mass gamma-glutamyltransferase in human bile is converted by physiological concentrations of the bile salts glycocholate and glycochenodeoxycholate to a form with a molecular mass estimated by gel chromatography to be 165,000. A molecule of intermediate molecular mass estimated to be 330,000 is obtained following treatment with the non-ionic detergent Triton X-100. When human bile is centrifuged at 150,000 X g, between 25-73% of gamma-glutamyltransferase activity is recovered in the supernatant. This proportion is increased following prior addition of bile salts to the bile. Analogous results are obtained for the high molecular mass enzymes alkaline phosphatase and leucine aminopeptidase, present in human bile, and also considered to originate from the hepatocyte plasma membrane. From these results it is suggested that these high molecular mass enzymes found in bile may, in part at least, represent artefacts following aggregation of the enzymes in aqueous media containing no bile salts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
303-13
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
The nature of gamma-glutamyltransferase and other hepatocyte plasma membrane enzymes in human bile.
pubmed:publicationType
Journal Article