Linked Life Data

8096396

Source:http://linkedlifedata.com/resource/pubmed/id/8096396

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-4-30
pubmed:abstractText
The clearance and organ uptake of gamma-glutamyltransferase was studied by injecting the purified human liver enzyme intravenously in the rat. The enzyme was almost exclusively taken up by liver hepatocytes with a rapid initial uptake. The clearance was significantly inhibited by asialofetuin as well as by galactose and fucose. The uptake of neuraminidase-treated enzyme was much more rapid than that of the native enzyme. Subfractions of gamma-glutamyltransferase obtained by lectin affinity chromatography revealed significant differences in clearance rates. The data strongly indicates that the uptake of circulating gamma-glutamyltransferase involves the galactose (asialo-glycoprotein) receptor of the parenchymal cells, and that the heterogeneity of gamma-glutamyltransferase results in varying clearance rates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
1156
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
283-7
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Clearance of circulating gamma-glutamyltransferase by the hepatic galactose receptor. Variability in clearance rate due to carbohydrate heterogeneity of the enzyme.
pubmed:affiliation
Institute of Medical Biology, University of Tromsø, Norway.
pubmed:publicationType
Journal Article