| Literature DB >> 3476488 |
H Marquardt, M N Lioubin, T Ikeda.
Abstract
The complete amino acid sequence of human type beta 2 transforming growth factor (hTGF-beta 2) was determined by automated Edman degradation of S-pyridylethylated hTGF-beta 2 and selected fragments. Cleavage of hTGF-beta 2 by enzymatic and chemical techniques established all the fragments in an unambiguous sequence. Human TGF-beta 2 consists of two disulfide-linked, identical subunits. Each hTGF-beta 2 subunit is a single-chain polypeptide of 112 residues, with a calculated molecular weight of 12,720. Human TGF-beta 2 displays 71.4% sequence homology with the functionally related human TGF-beta 1, and is distantly related (23-40% amino acid identity) to porcine inhibins and activins, the carboxyl-terminal regions of human Müllerian inhibiting substance, and the putative decapentaplegic gene complex protein of Drosophila.Entities:
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Year: 1987 PMID: 3476488
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157