ULTRACYTOCHEMICAL STUDY OF ALCOHOL DEHYDROGENASE ACTIVITY IN NORMAL MOUSE HEPATIC CELLS
1979 年 12 巻 4 号 p. 368-382
詳細
1979 年 12 巻 4 号 p. 368-382
The localization of alcohol dehydrogenase (ADH) activity in the hepatic (parenchymal) cells of normal mice was studied ultracytochemically by both the copper ferrocyanide and the tetranitroblue tetrazolium (TNBT) methods.
Reaction products, copper ferrocyanide showing the enzymatic activity, were mainly found in the cytoplasmic matrix immediately adjacent to the rough-surfaced endoplasmic reticulum (rER). In addition, the reaction products were also observed on the inner and outer membranes of mitochondria, cristae mitochondriales, and in the rER.
The reaction was completely inhibited by pyrazole (20 to 60mM), but only partially by N-ethylmaleimide (30 to 60mM).
The results obtained by the TNBT method were not necessarily identical to those obtained by the copper ferrocyanide method and the probable causes of different findings obtained by the two methods are also discussed.
