Isolation and characterization of a glycopeptide from human senescent erythrocytes

✍ Scribed by Curtis J. Henrich; David Aminoff

• Publisher: Elsevier Science
• Year: 1983
• Tongue: English
• Weight: 810 KB
• Volume: 120
• Category: Article
• ISSN: 0008-6215
• DOI: 10.1016/0008-6215(83)88006-9

✦ Synopsis

A glycopeptide (called "senescence-factor glycopeptide", SF-G) has been isolated from a tryptic digest of human erythrocytes by specific adsorption and elution from immobilized peanut lectin. SF-G was detectable in old but not in young erythrocytes isolated from the same unit of blood. It is present in small quantities, <l% of the D-galactose oxidase-borotritide-labeled D-gaiactosyl residues of erythrocytes. SF-G is free of sialic acid but is quite distinct from a similar glycopeptide isolated from completely desialylated erythrocytes. SF-G binds to spleen monocytes, and this property is aboIished upon treatment of SF-G with /3-galactosidase. Some, but not all, of the oligosaccharide chains of the SF-G are of the O-glycosyl type, being released by an endo-N-acetyl-cu-D-galactosaminidase.