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The purification of a detergent-soluble glucose-6-phosphatase from rat liver.
- Source :
-
European Journal of Biochemistry . 9/15/92, Vol. 208 Issue 3, p643-650. 8p. - Publication Year :
- 1992
-
Abstract
- A highly active and soluble glucose-6-phosphatase has been purified to near homogeneity from rat liver. Successful purification has been initiated by covalent labeling of the enzyme in native rat liver microsomes with pyridoxal 5′-phosphate and NaBH4, followed by solubilization of the microsomes with Triton X-100, chromatography on phenyl-Sepharose, hydroxyapatite, DEAE-Sephacel and a second chromatography step on hydroxyapatite. The final enzyme preparation obtained was approximately 700-fold purified over the activity of starting microsomes. As judged by SDS/PAGE the purified glucose-6-phosphatase is composed of a single protein with a molecular mass of 35 kDa. The present work demonstrates that the purified glucose-6-phosphatase must be arranged in the native microsomal membrane so that it is accessible to pyridoxal 5′-phosphate from the cytoplasmic side. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 208
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13684224
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1992.tb17230.x