HISTOCHEMISTRY AND BIOLOGY OF LEUCINE AMINOPEPTIDASES

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Histochemical detection for aminopeptidase in tissues and organs was made to employ aromatic substrates with conventional azo coupling method. Several amino acids combined with β-naphthylamide and aromatic amines with tosyl, carbasole and benzoyl groups were employed to histochemical use in the rat and guinea pig. Amino acids β-naphthylamide splitting enzymes were similarly localized histochemically despite of the use with several kinds of amino acids, though except for a few cases which were dipeptide β-naphthylamide. Enzymatic activities were intensely localized at the proximal convoluuted tubules, intermediate in distal tubules and tracable in glomerulus in the kidney, and they were restricted at villi of small intestine, as previously described (18) There were a few differences in distribution between the rat and guinea pig, i.e., in the rat kidney the outer zone of cortex was more reactive than the inner zone, however, in the guinea pig the inner zone was more marked to outer zone. Histochemical stainability of tissue sections were stronger in the guinea pig than those of the rat. The substrate specificity of aminopeptidase in the rat kidney was obtained to plot the two type Lineweaver-Burk curves. An optimal pH of the enzyme was detected ranging from 6.0 to 7.0 in the rat kidney. Zymogram from the rat kidney and small intestine using thin layer polyacrylamide gel electrophoresis showed two migrating bands with L-leucine β-naphthylamide. Zymogram for serum revealed a sharp band at anodal site and unclear two bands at the γ-globulin site.
日本組織細胞化学会の論文

HISTOCHEMISTRY AND BIOLOGY OF LEUCINE AMINOPEPTIDASES

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