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. 1960 Apr 1;7(2):261–264. doi: 10.1083/jcb.7.2.261

Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide

Marvin M Nachlas 1, Benito Monis 1, David Rosenblatt 1, Arnold M Seligman 1
PMCID: PMC2224813  PMID: 14425685

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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