Liver plasma membrane enzyme activities following glutaraldehyde fixation

P. J. Hertzog, R. N. Le Page, P. S. Bhathal

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The Wachstein-Meisel ATPase histochemical method has been previously used to demonstrate the ultrastructural localization of this enzyme in both whole liver and isolated plasma membranes following fixation in glutaraldehyde. Inthe present study biochemical assays of liver plasma membrane enzymes following fixation in cold 2.5% glutaraldehyde showed that approximately 40% of Mg2+ -ATPase, but only 4% of (Na+-K+)-ATPase activity remained in membranes from either control or ANIT-treated rats In addition, 5′-nucleotidase activity was almost abolished by fixation. The present results indicate that the Wachstein-Meisel method, when applied to biliary canaliculi, can reliably be used to demonstrate the ultrastructural, histochemical localization of Mg2+-ATPase but not that of(Na+-K+)-ATPase. Furthermore, the method permits a validcomparison to be made of the relative Mg2+ -ATPase activity in normal and chemically damaged biliary canaliculi.

Original languageEnglish
Pages (from-to)43-45
Number of pages3
Issue number1
Publication statusPublished - 1 Jan 1976
Externally publishedYes

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