Biochem J
Centre for Research into Human Development, University of Dundee Medical School, Ninewells Hospital, Scotland, U.K.
Published: April 1991
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.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1150023 | PMC |
http://dx.doi.org/10.1042/bj2750133 | DOI Listing |
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