Work

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

Year: 1960

Type: article

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.

Source: The Journal of Cell Biology

DOI: 10.1083/jcb.7.2.261

Authors: Marvin M. Nachlas, Benito Monis, David Rosenblatt, Arnold M. Seligman

Institutions: Johns Hopkins University, Sinai Hospital

Language: English

Topic: Peptidase Inhibition and Analysis

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W2105216834

FWCI: 2.217

Cites: 14

Cited by: 313

Related to: 9