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. 1980 Jun 1;187(3):719-25.
doi: 10.1042/bj1870719.

The isolation of human-erythrocyte band-3 polypeptide labelled with a photosensitive hydrophobic probe

E Wells, J B Findlay

The isolation of human-erythrocyte band-3 polypeptide labelled with a photosensitive hydrophobic probe

E Wells et al. Biochem J. .

Abstract

To investigate the intramembranous domains of the major band-3 polypeptide, human erythrocyte membranes were labelled with 1-azido-4-[125I]iodobenzene. The anion-exchange protein has been isolated by a new procedure that decreases possible contamination by other integral membrane proteins of similar molecular weight. After chemical modification, the protein was subjected to proteolytic cleavage by several proteinases to yield a distinct pattern of peptides, a few of which contained radioactivity.

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