Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide
Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide
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使用新底物 L-亮氨酰-4-甲氧基-2-萘酰胺改善亮氨酸氨肽酶的组织化学定位
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发表时间：
1960
期刊：
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通讯作者：
A. Seligman
中科院分区：
文献类型：
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作者：
M. Nachlas;B. Monis;D. Rosenblatt;A. Seligman
以l-亮氨酸-4-甲氧基-2-萘酰胺为底物，建立了亮氨酸氨基肽酶冷冻切片组织化学鉴定的新方法。优越的酶定位是由于与2-萘胺本身相比，水解产物4-甲氧基-2-萘胺的偶联速度更快，并且与四氮化二正氨基偶联后形成的染料的铜螯合物具有低脂溶性和高蛋白质质的特性。对新旧方法进行了比较，并描述了亮氨酸氨基肽酶在大鼠和人组织中的定位。
A new method for the histochemical demonstration of leucine aminopeptidase in fresh frozen sections was developed with the substrate L-leucyl-4-methoxy-2-naphthylamide. The superior enzyme localization is due to the more rapid rate of coupling of the hydrolysis product, 4-methoxy-2-naphthylamine as compared to 2-naphthylamine itself, and to the low lipid solubility and high substantivity for protein of the copper chelate of the dye formed on coupling with tetrazotized diorthoanisidine. A comparison of the old and the new method is illustrated, and a description is given of the localization of leucine aminopeptidase in the tissues of the rat and man.