Linde A, Bhown M, Cothran W C, Höglund A, Butler W T
Biochim Biophys Acta. 1982 Jun 4;704(2):235-9. doi: 10.1016/0167-4838(82)90151-0.
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.
通过阴离子交换色谱法,将大鼠牙本质中含γ-羧基谷氨酸(Gla)的蛋白质分离成四个密切相关的组分(γ1-γ4)。γ2的埃德曼降解产生了两个NH2末端序列,其中一个次要序列比主要序列短五个残基起始。γ2的凝胶电泳产生了一条主要蛋白带和一条次要蛋白带。γ3组分在凝胶电泳上产生一条带和一个单一的NH2末端序列。γ4的组成表明,与γ2和γ3相比,其COOH末端的一部分缺失。因此,大鼠牙本质含Gla蛋白质的一些异质性可以用末端缩短来解释。