Purification of rat heart and rat liver citrate synthases. Physical, kinetic, and immunological studies.

Purification of rat heart and rat liver citrate synthases. Physical, kinetic, and immunological studies.
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大鼠心脏和大鼠肝脏柠檬酸合酶的纯化。

DOI:
10.1016/s0021-9258(18)62217-3
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发表时间:
1971
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
P. Srere
P. Srere
中科院分区:
--
文献类型:
--
作者:
T. Moriyama;P. Srere

文献摘要

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从大鼠心脏和肝脏中分离纯化了柠檬酸合成酶。这些均质蛋白的分子量约为1 × 105,由两个明显相同的亚基组成。乙酰辅酶A和草酰乙酸的动力学常数以及两种酶的kifor ATP的动力学常数相同。利用大鼠心脏酶抗体进行的免疫学研究也表明,这两种酶是相同的。
The citrate synthases from rat heart and rat liver have been purified. These homogeneous proteins have a molecular weight of about 1 x 105and are composed of 2 apparently identical subunits. Kinetic constants for acetyl coenzyme A and oxaloacetate and theKifor ATP are the same for both enzymes. Immunological studies using antibody to the rat heart enzyme also indicate that the enzymes are identical.