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

A. Brovelli, G. Pallavicini, F. Sinigaglia, C. L. Balduini, C. Balduini

Research output: Contribution to journalArticlepeer-review

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, release a sialoglycopeptide, which contains glucosamine, galactosamine, galactose and mainly polar amino acids. Chemical composition, molecular size and aggregation properties suggest that this glycopeptide may be a fragment of glycophorin.

Original languageEnglish
Pages (from-to)497-500
Number of pages4
JournalBiochemical Journal
Volume158
Issue number2
Publication statusPublished - 1976

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Identification of a sialoglycopeptide released by self digestion from human erythrocyte membranes'. Together they form a unique fingerprint.

Cite this