Suttie J W, Hageman J M
J Biol Chem. 1976 Sep 25;251(18):5827-30.
Rat liver microsomes contain a vitamin K-dependent carboxylase activity that converts specific glutamyl residues of microsomal prothrombin precursor to gamma-carboxyglutamic acid residues. This activity has now been solubilized by treatment with Triton X-100. The pentapeptide, Phe-Leu-Glu-Glu-Val, has been synthesized; and it has been demonstrated that, in the presence of this peptide, the solubilized microsomes catalyze a vitamin K-dependent incorporation of added H14CO3- into a low molecular weight trichloroacetic acid-soluble compound. The carboxylated product has been identified as peptide-bound gamma-carboxyglutamic acid by its chemical stability during acidic and alkaline hydrolysis and by co-chromatography of an alkaline hydrolysate of the product with authentic gamma-carboxyglutamic acid. The conditions for peptide carboxylation appear to be identical with those demonstrated for precursor carboxylation.
大鼠肝脏微粒体含有一种维生素K依赖的羧化酶活性，该活性可将微粒体凝血酶原前体的特定谷氨酰残基转化为γ-羧基谷氨酸残基。现在，通过用曲拉通X-100处理，这种活性已被溶解。已合成五肽Phe-Leu-Glu-Glu-Val；并且已经证明，在该肽存在的情况下，溶解的微粒体催化添加的H14CO3-以维生素K依赖的方式掺入低分子量的三氯乙酸可溶性化合物中。通过其在酸性和碱性水解过程中的化学稳定性以及产物的碱性水解产物与 authenticγ-羧基谷氨酸的共色谱分析，已将羧化产物鉴定为肽结合的γ-羧基谷氨酸。肽羧化的条件似乎与前体羧化所证明的条件相同。
