Natural human tumor necrosis factor beta (lymphotoxin). Variable O-glycosylation at Thr super(7), proteolytic processing, and allelic variation

Natural human tumor necrosis factor beta (TNF- beta ) purified from supernatants of a human B-lymphoblastoid cell line was found to be heterogeneous in molecular mass, with components resolved by electrophoresis. All components are N-glycosylated at Asn super(62); N-glycosylation does not contribute...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1992-01, Vol.314 (1), p.85-88
Main Authors: Voigt, C G, Maurer-Fogy, I, Adolf, G R
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Natural human tumor necrosis factor beta (TNF- beta ) purified from supernatants of a human B-lymphoblastoid cell line was found to be heterogeneous in molecular mass, with components resolved by electrophoresis. All components are N-glycosylated at Asn super(62); N-glycosylation does not contribute to heterogeneity. In addition, part of the molecules are O-glycosylated at Thr super(7); O-glycosylation is heterogeneous due to variable decoration with neuraminic acid. The four lower molecular mass forms are derived from the full-length protein by trypsin-like proteolytic cleavage in the N-proximal region; these clipped molecules lack O-linked carbohydrates. Two allelic variants differing in amino acid position 26 (threonine/asparagine) were identified.
ISSN:0014-5793