Labelling of the intramembranous region of the major sialoglycoprotein of human erythrocytes with a photosensitive hydrophobic probe

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Abstract
Human erythrocyte membranes were incubated with the photosensitive hydrophobic reagent 1-azido-4-iodo[3H]benzene and the mixture was irradiated. The major sialoglycoprotein was then isolated and the labeled polypeptide was subjected to proteolytic dissection. Characterization of the purified tryptic and chymotryptic peptides showed that the probe was covalently attached only to the transmembrane region of the protein. This labeling pattern was discussed in relation to the use of such reagents for the identification of segments of membrane proteins exposed to the hydrophogic miliue of the membrane.