Kidney alanine: Glyoxylate aminotransferase isoenzymes; species distribution, subcellular distribution and properties
Kidney alanine: Glyoxylate aminotransferase isoenzymes; species distribution, subcellular distribution and properties
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肾丙氨酸：乙醛酸转氨酶同工酶；
DOI：
10.1016/0305-0491(80)90121-2
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发表时间：
1980
期刊：
影响因子：
--
通讯作者：
T. Noguchi
中科院分区：
文献类型：
--
作者：
Y. Takada;T. Noguchi
1. 1. 研究了不同哺乳动物物种肾亚细胞部分中 L-丙氨酸：乙醛酸转氨酶的分布。在匀浆中，猪、大鼠、猴、狗和猫的活性相对较高，而小鼠的活性较低。人类肾脏几乎没有检测到活性。大多数活性存在于猪、大鼠、猴、狗和猫的线粒体和可溶性部分中。 2. 2. 线粒体提取物含有两种形式的丙氨酸：狗和猫体内的乙醛酸转氨酶：其中一种称为同工酶 1，分子量约为 80,000，在这两个物种中均占主导地位；另一种称为同工酶2，分子量约为。 175,000。相比之下，大鼠、猪和猴肾线粒体中仅含有同工酶2。 3. 3. 同工酶1是从狗和猫的肾线粒体提取物中纯化的，同工酶2是从大鼠、猪和猴的肾线粒体提取物中纯化的。两种同工酶 1 制剂对以乙醛酸作为氨基受体的 L-丙氨酸和 L-丝氨酸具有特异性。获得了这两种同工酶 1 与 L-丝氨酸：丙酮酸转氨酶相同的证据。所有三种同工酶 2 制剂均对 L-丙氨酸和乙醛酸具有特异性。 4. 4. 描述了同工酶 1 和 2 的一些其他性质。
1. 1. The distribution of l-alanine: glyoxylate aminotransferase in the subcellular fractions of kidney was investigated with different mammalian species. In homogenates, the activity was relatively high in pig, rat, monkey, dog and cat, and low in mouse. Little or no activity was detected with human kidney. Most of the activity was present both in the mitochondria and in the soluble fraction in pig, rat, monkey, dog and cat. 2. 2. Mitochondrial extracts contained two forms of alanine: glyoxylate aminotransferase in dog and cat: one, designated isoenzyme 1, had a molecular weight of approx 80,000 and predominated in both species; the other, designated isoenzyme 2, had a molecular weight of approx. 175,000. In contrast, only isoenzyme 2 was contained in rat, pig and monkey kidney mitochondria. 3. 3. Isoenzyme 1 was purified from kidney mitochondrial extracts of dog and cat, and isoenzyme 2 from those of rat, pig and monkey. The two isoenzyme 1 preparations were specific for l-alanine and l-serine with glyoxylate as amino acceptor. Evidence that these two isoenzymes 1 are identical with l-serine: pyruvate aminotransferase was obtained. All three isoenzyme 2 preparations were specific for l-alanine and glyoxylate. 4. 4. Some other properties of isoenzymes 1 and 2 are described.