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PMID: 14425685 Published · ppublish English Journal Article

Improvement in the histochemical localization of leucine aminopeptidase with a new substrate, L-leucyl-4-methoxy-2-naphthylamide.

The Journal of biophysical and biochemical cytology ·Vol. 7 ·1960-04-00 ·Pages 261-4

NACHLAS MM, MONIS B, ROSENBATT D, SELIGMAN AM

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.

Keywords
NAPHTHALENES/chemistry PROTEASES/chemistry
MeSH Terms
2-Naphthylamine Aminopeptidases Animals Endopeptidases Humans Hydrolysis Leucyl Aminopeptidase Male Naphthalenes/chemistry Peptide Hydrolases/chemistry Rats Solubility
Chemicals
Naphthalenes 2-naphthylamide 4-methoxy-2-naphthylamine 2-Naphthylamine Endopeptidases Peptide Hydrolases Aminopeptidases Leucyl Aminopeptidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
NACHLAS M M
MONIS B
ROSENBATT D
SELIGMAN A M
References (11)
11 references, click to expand
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    Am J Med Sci. 1959 Nov;238:598-609 PMID: 13794557
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    Arch Biochem Biophys. 1955 Aug;57(2):458-74 PMID: 13259661
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    J Histochem Cytochem. 1956 May;4(3):217-26 PMID: 13332234
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    Obstet Gynecol. 1959 Oct;14:488-90 PMID: 14446470
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Article Info
Journal
The Journal of biophysical and biochemical cytology
Abbr.
J Biophys Biochem Cytol
ISSN
0095-9901
Published
1960-04-00
Pages
261-4
Language
English
Region
United States
NLM ID
17840020R
PMCID
PMC2224813
Subset
OM
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