Natural human tumor necrosis factor beta (lymphotoxin). Variable O-glycosylation at Thr7, 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 seven components resolved by gel electrophoresis. All components are N-glycosylated at Asn62; N-glycosylation does not contribute to heterogeneity. In addition, part of the molecules are O-glycosylated at Thr7; 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.
Voigt
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CG
Ernst Boehringer-Institut für Arzneimittelforschung, Bender & Co. GmbH, Vienna, Austria.
Maurer-Fogy
I
I
Adolf
G R
GR
D000483:Alleles; D000595:Amino Acid Sequence; D001216:Asparagine / Q000378:metabolism; D001402:B-Lymphocytes / Q000737:chemistry*; D014644:Genetic Variation; D006031:Glycosylation; D006801:Humans; D008233:Lymphotoxin-alpha / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D009438:Neuraminic Acids / Q000032:analysis; D011499:Protein Processing, Post-Translational; D013912:Threonine / Q000378:metabolism
D008233:Lymphotoxin-alpha; D009438:Neuraminic Acids; D013912:Threonine; D001216:Asparagine