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

Marvin M. Nachlas | Zendy; Benito Monis | Zendy; David S. Rosenblatt | Zendy; Arnold M. Seligman | Zendy

Open Access

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

Author(s) -

Marvin M. Nachlas,

Benito Monis,

David S. Rosenblatt,

Arnold M. Seligman

Publication year - 1960

Publication title -

the journal of cell biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.414

H-Index - 380

eISSN - 1540-8140

pISSN - 0021-9525

DOI - 10.1083/jcb.7.2.261

Subject(s) - aminopeptidase , leucine , biology , substrate (aquarium) , biochemistry , naphthylamine , enzyme , hydrolysis , leucyl aminopeptidase , amino acid , organic chemistry , chemistry , ecology

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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