Genetic variation as a tool for histochemical localization of a nonspecific esterase.
A prominent esterase activity was demonstrated histochemically in the straight portion of the proximal tubules in kidney of the mouse strain DBA/2J after inhibition with bis-p-nitrophenyl phosphate and subsequent staining, using 5-bromoindoxyl acetate as substrate. In the strain PUC/1Fre, the corresponding esterase was only weakly expressed. By comparing data from the literature (von Deimling et al. 1981) with the characteristic features of this kidney esterase including substrate preference, sensitivity to inhibitors, solubility, histochemical location, and strain differences, it was concluded that it was identical with the previously electrophoretically defined esterase-16.
von Deimling
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Ludwig-Aschoff-Haus, Pathologisches Institut, Universität Freiburg, Federal Republic of Germany.
D000818:Animals; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D005260:Female; D014644:Genetic Variation; D006651:Histocytochemistry; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D009596:Nitrophenols / Q000494:pharmacology
D007527:Isoenzymes; D009596:Nitrophenols; C002887:bis(4-nitrophenyl)phosphate; D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase