正常和患病人类肌肉中的芳基酰胺酶

Arylamidases in normal and diseased human muscle.

作者信息

Kar N C, Pearson C M

出版信息

Clin Chim Acta. 1976 Jun 1;69(2):311-5. doi: 10.1016/0009-8981(76)90510-6.

Abstract

Human skeletal muscle homogenates were found to contain enzymes that catalyze the hydrolysis of beta-naphthylamides of leucine, arginine and lysine, known substrates for neutral and basic arylamidases. They also contained a trace of activity towards alpha-aspartyl-beta-naphthylamide. The muscle arylamidases were found to be inhibited by p-chloromercuribenzoate, Hg2+ and puromycin. Leucyl, arginyl and lysysl arylamidases were slightly activated by cobalt ions. When compared to controls, no significant differences in muscle arylamidase activities were observed in patients with muscular dystrophies and certain denervating diseases.

摘要

研究发现，人类骨骼肌匀浆中含有可催化亮氨酸、精氨酸和赖氨酸的β-萘酰胺水解的酶，这些是中性和碱性芳基酰胺酶的已知底物。它们对α-天冬氨酰-β-萘酰胺也有微量活性。发现肌肉中的芳基酰胺酶会受到对氯汞苯甲酸、汞离子和嘌呤霉素的抑制。钴离子可使亮氨酰、精氨酰和赖氨酰芳基酰胺酶略有激活。与对照组相比，肌肉营养不良患者和某些失神经疾病患者的肌肉芳基酰胺酶活性未观察到显著差异。