Linked Life Data

972145

Source:http://linkedlifedata.com/resource/pubmed/id/972145

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1976-12-3
pubmed:abstractText
125I-Concanavalin A was found to bind to purified Golgi membranes in a manner which was time-dependent, proportional to the amount of Golgi protein, saturable, and inhibited by alpha-methyl-D-glucoside and unlabeled concanavalin A. Approximately 2 nmol of 125I-concanavalin A were bound per mg of membrane protein with a mean Ka of 0.2 x 10(7) M-1. After binding of concanavalin A to the membranes, all unbound lectin was removed by repeated washing prior to assay of galactosyltransferase activity to assure that bulk concanavalin A would not bind to the sugar acceptor during the enzyme assay. Therefore, the effects of the lectin were not due to altered acceptor concentrations in the assay. As a result of concanavalin A binding the activity of the galactosyltransferase of these membranes was enhanced by 70 to 100%. The enhancement was abolished by treatment of the concanavalin A-bound Golgi with alpha-methylglucoside. Kinetically this stimulation was reflected as an altered Km for N-acetylglucosamine and UDP-galactose. The data are suggestive that the stimulation of the enzyme results indirectly from perturbation of the membranes on binding of the lectin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
251
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5860-5
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Concanavalin A binding to membranes of the Golgi apparatus and resultant modification of galactosyltransferase activity.
pubmed:publicationType
Journal Article