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Headgroup dynamics of an integral membrane glycoprotein

1979; Elsevier BV; Volume: 90; Issue: 3 Linguagem: Inglês

10.1016/0006-291x(79)91906-5

1090-2104

Pat M. Lee, Chris W.M. Grant,

Erythrocyte Function and Pathophysiology

Glycophorin, an integral membrane glycoprotein known to be a receptor for several lectins, has been spin labelled specifically on headgroup terminal sugars. The labelled derivative has been studied in solution and also in various model membranes in an attempt to determine the factors which control headgroup dynamics. Under conditions which mimic those in a living cell the oligosaccharide chains show a uniform, relatively high freedom of motion, with individual sugar correlation times on the order of 6 × 10−10 sec to 8 × 10−10 sec depending upon the extent of glycoprotein headgroup involvement with other glycocalyx components. They exhibit no detectable occupancy of lipid or protein hydrophobic domains. Oligosaccharide dynamics are insensitive to factors which act upon that portion of the polypeptide backbone which inserts into the membrane, however a specific recognition event markedly reduces terminal sugar mobility.