Histochemical demonstration of an LNA-splitting enzyme in the cerebellum of the rat. A aminopeptidase-like reaction localized selectively in the granular layer with acid pH optimum.

R. Albrechtsen, H. Jensen
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引用次数: 5

Abstract

Histochemical investigations of leucine aminopeptidase using LNA (L-leucyl-beta-napthylamide) as a substrate reveals a marked enzyme activity selectively localized to the granular layer with inconspicuous reaction in the stratum moleculare and the Purkinje cells in the rat cerebellum. The LNA-splitting enzyme differs from the well-known leucine aminopeptidase (LAP) by its optimum at pH 5.5. The necessary long incubation period used in the present study, and its focal precipitation of the enzyme reaction product in the same place, like acid phosphatases, in the granular layer, suggest a lysosomal localization. The functional role of the LNA-splitting enzyme has been discussed; it is considered that it is involved not only in the protein transformation for synaptic function, but may perhaps also play an important pathogenic role in necrosis, atrophy or even autolysis.
大鼠小脑中na分裂酶的组织化学证明。一种类似氨基肽酶的反应,选择性地定位于酸性pH最适宜的颗粒层。
以LNA (l- leucyl- β -napthylamide)为底物对亮氨酸氨基肽酶进行组织化学研究发现,亮氨酸氨基肽酶在大鼠小脑颗粒层中选择性定位,在层分子和浦肯野细胞中反应不明显。lna分裂酶不同于众所周知的亮氨酸氨基肽酶(LAP),它在pH为5.5时达到最佳状态。本研究使用了必要的长潜伏期,并且酶反应产物在颗粒层的同一位置集中沉淀,如酸性磷酸酶,表明溶酶体定位。讨论了rna分裂酶的功能作用;据认为,它不仅参与突触功能的蛋白质转化,而且可能在坏死、萎缩甚至自溶中起重要的致病作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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