1982
DOI: 10.1021/bi00259a018
|View full text |Cite
|
Sign up to set email alerts
|

Monosaccharide transporter of the human erythrocyte. Characterization of an improved preparation

Abstract: The human erythrocyte monosaccharide transporter has been purified through the use of the dialyzable detergent octyl glucoside. It was found that the transporter denatures in the detergent and that the rate of this process could be reduced by increasing the ratio of phospholipid to detergent. The transporter was obtained in higher yield and with a higher specific activity for cytochalasin B binding than has been previously reported. Scatchard plot analysis of cytochalasin B binding to the reconstituted prepara… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
103
0

Year Published

1984
1984
2001
2001

Publication Types

Select...
6
2

Relationship

0
8

Authors

Journals

citations
Cited by 211 publications
(104 citation statements)
references
References 39 publications
1
103
0
Order By: Relevance
“…Chemicals and radiochemicals used were from the following sources: Na35SO4 (25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40) (10.7 Ci/nmol) from New England Nuclear. Stractan (arabino galactan) from Sigma.…”
Section: Methodsmentioning
confidence: 99%
See 1 more Smart Citation
“…Chemicals and radiochemicals used were from the following sources: Na35SO4 (25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40) (10.7 Ci/nmol) from New England Nuclear. Stractan (arabino galactan) from Sigma.…”
Section: Methodsmentioning
confidence: 99%
“…The other native transport function of band 3 [27,37,38] or band 4.5 [39][40][41], which are both present in the vesicles, is D-glucose transport. To check whether this transport function in the recombinant vesicles is intact, two approaches have been followed.…”
Section: Specific Permeability Properties Of Erythrocyte Lipidband 3 mentioning
confidence: 99%
“…Purified glucose transport protein from cells incubated with [3H]palmitate showed labeling of a broad peak in the band 4.5 region corresponding to that expected for the glucose transporter [14]. Although not clearly separated from the tracking dye in the 8°7o acrylamide gel of Fig.…”
Section: Resultsmentioning
confidence: 90%
“…Labeled cells were lysed immediately, leaky ghost membranes prepared [10], and these depleted of extrinsic membrane proteins as described by Gorga and Lienhard [13]. Purified glucose transporter was prepared as described by Baldwin et al [14]. The labeled glucose transport protein was immunoprecipitated from purified band 4.5 as described by Tai and Carter-Su [15], using monoclonal antibody 7F7.5 coupled to Protein A-Sepharose CL-4B [16].…”
Section: Methodsmentioning
confidence: 99%
“…The cDNA-deduced amino acid sequences of six GLUT isoforms (Mueckler et al, 1985;Kayano et al, 1988;Asano et al, 1989;James et al, 1989;Kayano et al, 1990), together with the biochemical data obtained from purified GLUT1 protein (Kasahara and Hinkle, 1976;Baldwin et al, 1982;Cairns et al, 1987;Alvarez et al, 1987) indicate that all of these isoforms share a common transmembrane topology, having a large (about 50% of protein mass) transmembrane domain, with two grossly asymmetric nonmembrane domains, the cytoplasmic domain (about 35% of protein mass) and the exoplasmic domain (Figure 1). The trans- …”
Section: Transmembrane Topology Common To All Glut Isoformsmentioning
confidence: 98%