COMPARISON OF FIXATIVES AND SUBSTRATES FOR AMINOPEPTIDASE
Open Access
- 1 July 1965
- journal article
- research article
- Published by SAGE Publications in Journal of Histochemistry & Cytochemistry
- Vol. 13 (6) , 503-509
- https://doi.org/10.1177/13.6.503
Abstract
Although aminopeptidase activity is extensively inhibited by glutaraldehyde, it is sufficiently well preserved after brief glutaraldehyde fixation for histochemical use in active tissues in contrast to the too great losses with comparable formaldehyde-fixation. The localization of histochemical activity is sharper with glutaraldehyde-fixed frozen sections than with fresh frozen sections in many tissues though not all, and both methods are better than with formalin fixed tissue. Comparison of the results with leucyl, methionyl and alanyl amides of the rapid coupler, 4-methoxy-2-naphthylamine, showed exactly the same localization.This publication has 2 references indexed in Scilit:
- CYTOCHEMISTRY AND ELECTRON MICROSCOPYThe Journal of cell biology, 1963
- An evaluation of aminopeptidase specificity with seven chromogenic substratesArchives of Biochemistry and Biophysics, 1962