| Literature DB >> 7104368 |
A Linde, M Bhown, W C Cothran, A Höglund, W T Butler.
Abstract
With anion-exchange chromatography, the gamma-carboxyglutamic acid (Gla)-containing proteins of rat dentin were separated into four closely related fractions (gamma 1-gamma 4). Edman degradation of gamma 2 gave two NH2-terminal sequences with a minor sequence beginning five residues shorter than the major one. Gel electrophoresis of gamma 2 yielded one major and one minor protein band. Fraction gamma 3 gave one band on gel electrophoresis and a single NH2-terminal sequence. The composition of gamma 4 suggested that, compared to gamma 2 and gamma 3, a portion of the COOH-terminal was missing. Thus some of the heterogeneity of rat dentin Gla-containing proteins can be explained by shortened ends.Entities:
Mesh:
Substances:
Year: 1982 PMID: 7104368 DOI: 10.1016/0167-4838(82)90151-0
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002