Purification and properties of glycine decarboxylase, a component of the glycine cleavage system, from rat liver mitochondria and immunochemical comparison of this enzyme from various sources.
Purification and properties of glycine decarboxylase, a component of the glycine cleavage system, from rat liver mitochondria and immunochemical comparison of this enzyme from various sources.
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来自大鼠肝线粒体的甘氨酸脱羧酶（甘氨酸裂解系统的一个组成部分）的纯化和特性以及来自不同来源的该酶的免疫化学比较。
DOI：
10.1093/oxfordjournals.jbchem.a133074
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发表时间：
1980
期刊：
影响因子：
--
通讯作者：
G. Kikuchi
中科院分区：
文献类型：
--
作者：
K. Hayasaka;H. Kochi;K. Hiraga;G. Kikuchi
甘氨酸脱羧酶，暂称为P-蛋白作为甘氨酸裂解系统的组成部分，纯化到接近同质性从大鼠肝线粒体。纯化的P-蛋白是分子量约为210，000的同源二聚体，由分子量为105，000的相同亚基组成。在纯化的P蛋白催化的甘氨酸羧基碳与CO_2交换反应中，在H蛋白存在下，最适pH为6.7，对甘氨酸的Km为6.6mM，对H蛋白的Km为7.4 μ M。制备了抗大鼠肝P蛋白的特异性兔抗体。Ouchterlony双扩散分析和免疫抑制实验表明，该抗体的免疫交叉反应的P-蛋白从不同物种的动物，如鲤鱼，青蛙，蛇，鸡，牛，和人类，这表明一个相当保守的进化的甘氨酸切割系统。
Glycine decarboxylase, tentatively called P-protein as a constituent of the glycine cleavage system, was purified to near homogeneity from rat liver mitochondria. The purified P-protein was a homodimer with a molecular weight of about 210,000, consisting of identical subunits with a molecular weight of 105,000. In the exchange reaction of the carboxyl carbon of glycine wih CO2 catalyzed by the purified P-protein in the presence of H-protein, the pH optimum was 6.7, Km for glycine was 6.6 mM, and Km for H-protein was 7.4 microM. A specific rabbit antibody against the purified rat liver P-protein was prepared. Ouchterlony double diffusion analysis and immunoinhibition experiments using this antibody revealed immunological cross-reactivity among the P-proteins from various species of animals such as carp, frog, snake, chicken, bovine, and human, suggesting a quite conservative evolution of the glycine cleavage system.