Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1983-10-8
pubmed:abstractText
Band 3 and the diffuse component of zone 4.5, designated band 4.5.B, have been separately prepared from human erythrocyte membranes and incorporated into the membranes of 150 nm 1-palmitoyl-2-oleoyl phosphatidylcholine vesicles. The rates of glucose influx into these vesicles were measured under zero-trans conditions. Both sets of vesicles exhibited substrate-saturable transport which was inhibited by phloretin. However, the specific activity of the band 3 vesicles, 292 mumol X min-1 X (mg protein)-1, was more than twice that of the band 4.5.B vesicles, and the turnover number of transporters in the band 3 vesicles was at least 4-fold greater than those in the 4.5.B vesicles. Very little background density was visible in the band 4.5 region of erythrocyte membranes protected from degradation. In unprotected membranes, band 4.5.B was abundantly present, could be purified, and had glucose transport activity. Previously we have shown (Biochemistry 19, 1205 (1980] that maltosyl isothiocyanate, an affinity label for the glucose transporter, labelled a single 100 000 Mr protein of the intact erythrocyte membrane. Based upon the results of both affinity labelling and reconstitution we suggest that the native glucose transporter is a component of band 3, and that band 4.5.B contains a partially active fragment of the native transporter.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
733
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25-33
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Reconstitution of glucose transport using human erythrocyte band 3.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.