A review of time literature has revealed timat several autimors imave ascribed alkaline phosiihatase adtivitY to osteoclasts (l2)(15). Accoroling to time review of Hancox, it wouk! appear that suohi activity represenmts a diffusion artefact (13). Of course, it is possible that osteoclasts
Recently several chromogenic substrates for the demonstration of aminopeptidase have been described. The first, DL-alanyl-$-naphthylamide, was found to be hydrolyzed by a number of animal tissues and tissue fluids (8, 1 1). This substrate was also used for the histochemical demonstration of aminopeptidase in frozen sections. However, the sections had to be studied immediately since the dye reorganized into a coarse precipitate after 30 minutes (1 1). Another substrate, L-leucyl-fl-naphthylamide, was found to be hydrolyzed by tissue homogenates, and thus might also be useful as a histochemical reagent (8). Furthermore, leucine substrates appear to be more specific for leucine aminopeptidase as contrasted with alanyl compounds (5, 17). This study deals with the development and evaluation of a microscopic and quantitative histochemical method for aminopeptidase utilizing L-leucyl-f3-naphthylamide. A histochemical comparison is also made with the substrate DLalanyl-fl-naphthylamide.
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