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Natural human tumor necrosis factor beta (lymphotoxin) Variable O ‐glycosylation at Thr 7 , proteolytic processing, and allelic variation
Author(s) -
Voigt Christopher G.,
Maurer-Fogy Ingrid,
Adolf Günther R.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81467-z
Subject(s) - tumor necrosis factor alpha , lymphotoxin , lymphotoxin alpha , glycosylation , beta (programming language) , lymphotoxin beta receptor , allele , tumor necrosis factors , immunology , biology , microbiology and biotechnology , genetics , gene , computer science , programming language
Natural human tumor necrosis factor beta (TNF‐β) purified from supernatants of a human B‐lymphoblastoid cell line was found to be heterogeneous in molecular mass, with seven components resolved by gel electrophoresis. All components are N ‐glycosylate at Asn 62. , N ‐glycosylation does not contribute to heterogeneity. In addition, part of the molecules are O ‐glycosylated at Thr 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.