Histochemistry of lactic dehydrogenase in heart and pectoralis muscles of rat.
Histochemistry of lactic dehydrogenase in heart and pectoralis muscles of rat.
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DOI：
10.1083/jcb.51.3.621
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发表时间：
1971-12
影响因子：
7.8
通讯作者：
Sharma, H M
中科院分区：
文献类型：
--
作者：
Baba, N;Sharma, H M
本文对大鼠左心室肌和胸大肌的乳酸脱氢酶（LDH）同工酶进行了细胞内定位研究。在2%缓冲甲醛中固定组织2小时，提供了超微结构和酶活性的最佳保存。总LDH活性被发现弥漫在基质的肌浆和心肌线粒体。在骨骼肌中，肌浆网中观察到强烈反应，肌浆基质和线粒体中观察到中等活性。LDH同工酶的分化是通过加入4 M尿素或加热来完成的。心肌型同工酶主要分布于线粒体和肌浆，而肌肉型同工酶主要分布于骨骼肌的肌浆网。据推测，骨骼肌的肌浆网是无氧糖酵解的位点，肌浆和线粒体主要参与丙酮酸的有氧代谢。
Left-ventricular heart muscle and pectoralis major muscle of the rat were studied to determine the intracellular localization of lactic dehydrogenase (LDH) isoenzymes. Fixation of tissue for 2 hr in 2% buffered formaldehyde provided the best preservation of the ultrastructure and enzyme activity. Total LDH activity was found diffusely in the ground substance of the sarcoplasm and in the mitochondria of the heart muscle. In skeletal muscle a strong reaction was noted in the sarcoplasmic reticulum, and moderate activity was seen in the ground substance of the sarcoplasm and in the mitochondria. Differentiation of the isoenzymes of LDH was accomplished by addition of 4 M urea or application of heat. Heart-type isoenzymes were mainly localized in the mitochondria and sarcoplasm, whereas muscle-type isoenzymes were localized mainly in the sarcoplasmic reticulum of the skeletal muscle. It is speculated that the sarcoplasmic reticulum of the skeletal muscle is the site of anaerobic glycolysis and that the sarcoplasm and mitochondria are involved primarily in aerobic metabolism of pyruvate.