Autor: |
Linde A, Bhown M, Cothran WC, Höglund A, Butler WT |
Jazyk: |
angličtina |
Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 1982 Jun 04; Vol. 704 (2), pp. 235-9. |
DOI: |
10.1016/0167-4838(82)90151-0 |
Abstrakt: |
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. |
Databáze: |
MEDLINE |
Externí odkaz: |
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