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Histochemical method for dipeptidyl aminopeptidase II with a new anthraquinonyl hydrazide substrate.
Authors:A Dikov  M Dimitrova  T Pajpanova  R Krieg  K J Halbhuber
Institution:Institute of Experimental Morphology and Anthropology, Bulgarian Academy of Sciences, Sofia.
Abstract:A new method for the histochemical visualization of lysosomal aminopeptidase dipeptidyl peptidase II activity (DPP II) is developed. The substrate L-Lys-L-Ala-5-chloro-1-anthraquinonylhydrazide-2HBr (Lys-Ala-CAH) is readily hydrolyzed by the enzyme to release 5-Cl-1-anthraquinonylhydrazine (CAH). The last compound is simultaneously coupled to an aromatic aldehyde, e.g. 4-nitrobenzaldehyde (p-NBA) or piperonal (3,4-methylenedioxybenzaldehyde; PPL), to form a highly insoluble deeply colored hydrazone, marking the enzyme locations. Using the new method, DPP II is successfully localyzed in tissue sections from different rat organs.
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