d-Glucose Uptake by Isolated Human Erythrocyte Membranes versusd-Glucose Transport by Human Erythrocytes

Kahlenberg, Arthur; Dolansky, Donna; Rohrlick, Ruth

doi:10.1016/s0021-9258(19)45026-6

Cited by 24 publications

(1 citation statement)

References 19 publications

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“…Furthermore, evidence exists which suggests that there are approximately 300 000 copies of each transporter per cell (Avruch & Fairbanks, 1972; Ho & Guidotti, 1975), although the number of anion transporters is unsettled (Rakitzis et al, 1978). In addition, it has been reported that external proteolysis under conditions which lead to conversion of band 3 to fragments of approximately 55000 and 40000 molecular weight does not inhibit the functions of the transporters for glucose (Avruch et al, 1973;Carter et al, 1973;Kahlenberg et al, 1972), cations (Avruch & Fairbanks, 1972;Wagner et al, 1974), or anions (Rothstein et al, 1976). Despite these similarities, in intact cells each transport function appears to be independent of the others.…”

Section: Discussionmentioning

confidence: 99%

Maltosyl isothiocyanate: an affinity label for the glucose transporter of the human erythrocyte membrane. 2. Identification of the transporter

Mullins¹,

Langdon²

1980

Biochemistry

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Maltosyl isothiocyanate (MITC), a potent irreversible inhibitor of glucose transport in human erythrocytes [Mullins, R. E., & Langdon, R. G. (1980) Biochemistry (preceding paper in this issue)], has been found to react almost exclusively with band 3 of the human erythrocyte membrane. The incorporation of [14C]MITC into band 3 was found to be antagonized by transportable sugars or competitive inhibitors of transport. On the basis of [14C]MITC incorporation into band 3 and MITC inhibition of transport, it is estimated that there are 3 x 10(5) glucose transporters present in the erythrocyte membrane. It was found that [14C]MITC-labeled band 3 could be converted into 14C-labeled band 4.5 during the Triton X-100 extraction procedure described by Kasahara & Hinkle [Kasahara, M., & Hinkel, P. C. (1977) J. Biol. Chem. 252, 7384]. On the basis of the evidence presented here and in the preceding paper, it is suggested that in the native erythrocyte membrane a component of band 3 is the glucose transport protein and that during purification with nonionic detergents the transport protein may be enzymatically degraded with some retention of activity.

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Section: Discussionmentioning

confidence: 99%

Maltosyl isothiocyanate: an affinity label for the glucose transporter of the human erythrocyte membrane. 2. Identification of the transporter

Mullins¹,

Langdon²

1980

Biochemistry

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Properties and structural basis of simple diffusion pathways in the erythrocyte membrane

Deüticke¹

Reviews of Physiology, Biochemistry and Pharmacology

181

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Effect of trypsin, phospholipases, and membrane-impermeable reagents on the uptake of palmitic acid by isolated rat liver cells

Mahadevan¹,

Sauer²

1974

Archives of Biochemistry and Biophysics

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d-Glucose Uptake by Isolated Human Erythrocyte Membranes versusd-Glucose Transport by Human Erythrocytes

Cited by 24 publications

References 19 publications

Maltosyl isothiocyanate: an affinity label for the glucose transporter of the human erythrocyte membrane. 2. Identification of the transporter

Maltosyl isothiocyanate: an affinity label for the glucose transporter of the human erythrocyte membrane. 2. Identification of the transporter

Properties and structural basis of simple diffusion pathways in the erythrocyte membrane

Effect of trypsin, phospholipases, and membrane-impermeable reagents on the uptake of palmitic acid by isolated rat liver cells

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