CYTOCHEMICAL LOCALIZATION OF MG++-ATPASE AND CA++-ATPASE ON THE LIMITING MEMBRANE OF RAT LIVER PEROXISOMES

By a modified cytochemical staining procedure, Mg++- and Ca++-ATPase were clearly localized on the surface of the limiting membrane of peroxisomes in hepatocytes of the rat. The matrix and core structure (crystalloid) were devoid of the ATPase reaction. The reaction on the peroxisomal membrane was a...

Full description

Saved in:
Bibliographic Details
Published inACTA HISTOCHEMICA ET CYTOCHEMICA Vol. 23; no. 5; pp. 601 - 611
Main Authors MAKITA, TAKASHI, HAKOI, KAZUO, ARAKI, NOBUKAZU
Format Journal Article
LanguageEnglish
Published Kyoto JAPAN SOCIETY OF HISTOCHEMISTRY AND CYTOCHEMISTRY 01.01.1990
Japan Society of Histochemistry and Cytochemistry
Japan Science and Technology Agency
Subjects
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Rat
Enzyme
Liver
Rodentia
Enzyme inhibitor
Cytochemistry
Vertebrata
Mammalia
Transmission electron microscopy
Peroxisome
Ca-»ATPase
Localization
Mg-ATPase
Online AccessGet full text

Cover

More Information
Summary:By a modified cytochemical staining procedure, Mg++- and Ca++-ATPase were clearly localized on the surface of the limiting membrane of peroxisomes in hepatocytes of the rat. The matrix and core structure (crystalloid) were devoid of the ATPase reaction. The reaction on the peroxisomal membrane was abolished by an inhibitor of Mg++-ATPase, 10mM p-chloromercuric benzoate (PCMB) and by the omission of the substrate, ATP-2Na, or by replacement of it with β-glycerophosphate. The reaction was not suppressed by the inhibitor of a alkaline phosphatase, 2.5mM levamisole; by an inhibitor of Na-K-ATPase, 10mM ouabain. After replacement of MgSO4 by CaCl2, Ca-ATPase was localized at exactly the same site where Mg-ATPase was detected.
ISSN:0044-5991
1347-5800
DOI:10.1267/ahc.23.601