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

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...

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Detalles Bibliográficos
Autores principales: Nachlas, Marvin M., Monis, Benito, Rosenblatt, David, Seligman, Arnold M.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1960
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2224813/
https://www.ncbi.nlm.nih.gov/pubmed/14425685
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author Nachlas, Marvin M.
Monis, Benito
Rosenblatt, David
Seligman, Arnold M.
author_facet Nachlas, Marvin M.
Monis, Benito
Rosenblatt, David
Seligman, Arnold M.
author_sort Nachlas, Marvin M.
collection PubMed
description 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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spelling pubmed-22248132008-05-01 Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide Nachlas, Marvin M. Monis, Benito Rosenblatt, David Seligman, Arnold M. J Biophys Biochem Cytol Article 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. The Rockefeller University Press 1960-04-01 /pmc/articles/PMC2224813/ /pubmed/14425685 Text en Copyright © Copyright, 1960, by The Rockefeller Institute Press
spellingShingle Article
Nachlas, Marvin M.
Monis, Benito
Rosenblatt, David
Seligman, Arnold M.
Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide
title Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide
title_full Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide
title_fullStr Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide
title_full_unstemmed Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide
title_short Improvement in the Histochemical Localization of Leucine Aminopeptidase with a New Substrate, L-Leucyl-4-Methoxy-2-Naphthylamide
title_sort improvement in the histochemical localization of leucine aminopeptidase with a new substrate, l-leucyl-4-methoxy-2-naphthylamide
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2224813/
https://www.ncbi.nlm.nih.gov/pubmed/14425685
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