Identification of a sialoglycopeptide released by self-digestion from human erythrocyte membranes

Abstract

Membranes from human O Rhesus-positive erythrocyte ghosts were tested in vitro for their ability to digest their own glycoproteins. Ghost membranes incubated in Tris/HCl buffer, pH 7.4, released a sialoglycopeptide, which contained glucosamine, galactosamine, galactose and mainly polar amino acids. Chemical composition, molecular size and aggregation properties suggested that this glycopeptide may be a fragment of glycophorin.