Electron microscopical demonstration of glucose-6-phosphatase in native cryostat sections fixed with glutaraldehyde through semipermeable membranes

The cytochemical demonstration of glucose-6-phosphatase (G6Pase) activity in native cryostat sections fixed with glutaraldehyde through semipermeable membranes is superior to conventional methods with regard to exact localization and lack of inactivation and diffusion of the enzyme, together with si...

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Bibliographic Details
Published in:Histochemistry 1979, Vol.65 (1), p.41-47
Main Authors: Benner, U, Hacker, H J, Bannasch, P
Format: Article
Language:English
Subjects:
Animals
Bile Ducts, Intrahepatic - enzymology
Endoplasmic Reticulum - enzymology
Fixatives
Frozen Sections
Glucose-6-Phosphatase - analysis
Glutaral
Histocytochemistry - methods
Intracellular Membranes - enzymology
Liver - enzymology
Liver - ultrastructure
Membranes
Microscopy, Electron
Rats
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Summary:The cytochemical demonstration of glucose-6-phosphatase (G6Pase) activity in native cryostat sections fixed with glutaraldehyde through semipermeable membranes is superior to conventional methods with regard to exact localization and lack of inactivation and diffusion of the enzyme, together with simultaneous excellent preservation of the tissue fine structure. In rat liver not only hepatocytes but also many bile duct epithelia and endothelia of arterioles and venules show a marked G6Pase activity in the membranes of the endoplasmic reticulum including the nuclear envelope.
ISSN:0301-5564
1432-119X
DOI:10.1007/BF00496684