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. 1988 Dec 1;256(2):421–427. doi: 10.1042/bj2560421

Proteolytic dissection as a probe of conformational changes in the human erythrocyte glucose transport protein.

A F Gibbs 1, D Chapman 1, S A Baldwin 1
PMCID: PMC1135426  PMID: 3223921

Abstract

Tryptic digestion has been used to investigate the conformational changes associated with substrate translocation by the human erythrocyte glucose transporter. The effects of substrates and inhibitors of transport on the rates of tryptic cleavage at the cytoplasmic surface of the membrane have confirmed previous observations that this protein can adopt at least two conformations. In the presence of phloretin or 4,6-O-ethylidene-D-glucose, the rate of cleavage is slowed. Because these inhibitors bind preferentially at the extracellular surface of the transporter, their effects must result from a conformational change rather than from steric hindrance. A conformational change must also be responsible for the effect of the physiological substrate D-glucose, which is to increase the rate of cleavage. The regions of the protein involved in the conformational changes include both of the large cytoplasmic regions that are cleaved by trypsin: these are the central hydrophilic region of the sequence (residues 213-269) and the hydrophilic C-terminal region (residues 457-492).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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