Transverse topology of glucose-6-phosphatase in rat hepatic endoplasmic reticulum.
Antibodies raised against purified components of glucose-6-phosphatase were used to study the transmembrane orientation of the complex. Measurements of glucose-6-phosphatase activities and immunoblot analysis of sealed microsomes and detergent-solubilized microsomes after treatment with proteases suggested that most of the catalytic subunit resides within the lumen of the endoplasmic reticulum. In contrast, other components of glucose-6-phosphatase are accessible to the cytoplasm. Treatment of the partially purified glucose-6-phosphatase enzyme with glycopeptide N-glycosidase indicated that the catalytic subunit of the enzyme was a glycoprotein.
Waddell
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Centre for Research into Human Development, University of Dundee Medical School, Ninewells Hospital, Scotland, U.K.
Burchell
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A
D000818:Animals; D002118:Calcium / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D010450:Endopeptidases / Q000494:pharmacology; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D005952:Glucose-6-Phosphatase / Q000032:analysis* / Q000378:metabolism; D006031:Glycosylation; D015151:Immunoblotting; D046911:Macromolecular Substances; D008862:Microsomes, Liver / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains
D046911:Macromolecular Substances; D005952:Glucose-6-Phosphatase; D010450:Endopeptidases; D002118:Calcium