Howard J B, Nelsestuen G L
Proc Natl Acad Sci U S A. 1975 Apr;72(4):1281-5. doi: 10.1073/pnas.72.4.1281.
A 39-residue peptide from the tryptic digestion of bovine blood clotting factor X has been isolated by specific adsorption on barium citrate. The amino- and carboxyl-terminal sequences of the peptide were determined and compared to the vitamin K-dependent Ca2+-binding region from bovine prothrombin. The factor X peptide was found to contain gamma-carboxyglutamic acid residues, and the results of independent analysis are consistent with all 14 glutamic acid residues as gamma-carboxyglutamic acid. The similarity of the factor X peptide to the prothrombin peptide supports the hypothesis that the vitamin K-dependent blood clotting proteins are descended from a common ancestral gene.
通过特异性吸附于柠檬酸钡,从牛凝血因子X的胰蛋白酶消化产物中分离出了一段39个残基的肽段。测定了该肽段的氨基末端和羧基末端序列,并与牛凝血酶原的维生素K依赖型Ca2+结合区域进行了比较。发现因子X肽段含有γ-羧基谷氨酸残基,独立分析结果表明所有14个谷氨酸残基均为γ-羧基谷氨酸。因子X肽段与凝血酶原肽段的相似性支持了以下假说:维生素K依赖型凝血蛋白起源于一个共同的祖先基因。