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. 1991 Apr 1;275(Pt 1):133–137. doi: 10.1042/bj2750133

Transverse topology of glucose-6-phosphatase in rat hepatic endoplasmic reticulum.

I D Waddell 1, A Burchell 1
PMCID: PMC1150023  PMID: 1850236

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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