HETEROGENEITY OF ARGINASES IN RAT TISSUES
HETEROGENEITY OF ARGINASES IN RAT TISSUES
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DOI：
10.1042/bj1530469
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发表时间：
1976-01-01
影响因子：
4.1
通讯作者：
RAPER, SM
中科院分区：
文献类型：
--
作者：
HERZFELD, A;RAPER, SM
大鼠组织中的精氨酸酶 (EC 3.5.3.1) 反应由 3 种同工酶催化，可通过聚丙烯酰胺凝胶双向电泳将其分离。阳极电泳显示除颌下腺外的所有非肝组织中均存在迁移带（同工酶 I），而所有组织中均存在非迁移带。后者通过阴极电泳分解为同工酶 II（肝脏和颌下腺的特征）和存在于肾、肠和胰腺中的非移动带（同工酶 II）。在同一凝胶柱中对肝脏和肾脏提取物的混合物进行 2 个方向的连续电泳，分离出所有 3 种同工酶。来自不同组织的精氨酸酶的溶解特性、热敏感性和底物特异性的差异可能与其电泳行为相关。 L-刀豆氨酸可以代替精氨酸作为肾脏提取物中的底物，但不能代替肝脏提取物中的底物。两种肾同工酶对 L-刀豆氨酸的水解效果相同；来自颌下腺的同工酶 III 仅表现出非常低的活性。抗肝精氨酸酶的抗血清与来自颌下腺的酶相互作用，但不灭活或吸附来自肾、肠或胰腺的精氨酸酶。给出了16只正常成年大鼠组织中精氨酸酶的分布；改进的、灵敏的检测方法适用于肝活性低至 0.1% 的组织。
Arginase (EC 3.5.3.1) reactions in rat tissues were catalyzed by 3 isoenzymes which can be separated by bidirectional electrophoresis on polyacrylamide gels. Anodic electrophoresis reveals a migrating band (isoenzyme I) present in all non-hepatic tissues except submaxillary gland and a non-migrating band found in all tissues. The latter is resolved by cathodic electrophoresis into isoenzyme II (characteristic of liver and submaxillary gland) and a non-moving band (isoenzyme II), present in kidney, intestine and pancreas. Sequential electrophoresis, in 2 directions, of mixtures of liver and kidney extracts in the same gel columns separated all 3 isoenzymes. Differences in the solubilization properties, heat-sensitivity and substrate specificity of arginases from different tissues could be correlated with their electrophoretic behavior. L-Canavanine could replace arginine as substrate in extracts of kidney but not of liver. Both kidney isoenzymes hydrolyzed L-canavanine equally well; isoenzyme III from submaxillary gland showed only very low activity. Antiserum against liver arginase interacted with the enzyme from submaxillary gland, but did not inactivate or adsorb arginase from kidney, intestine or pancreas. The distribution of arginase among 16 normal adult rat tissues is presented; the improved, sensitive, assay method was applicable to tissues containing as little as 0.1% of the hepatic activity.