Crossref journal-article
Wiley
European Journal of Biochemistry (311)
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.

Bibliography

SPETH, M., & SCHULZE, H. (1992). The purification of a detergent‐soluble glucose‐6‐phosphatase from rat liver. European Journal of Biochemistry, 208(3), 643–650. Portico.

Authors 2
  1. Maria SPETH (first)
  2. Hans‐Ulrich SCHULZE (additional)
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Dates
Type When
Created 20 years, 5 months ago (March 4, 2005, 2:16 a.m.)
Deposited 1 year, 11 months ago (Oct. 1, 2023, 4:41 a.m.)
Indexed 1 year, 6 months ago (Feb. 29, 2024, 12:26 p.m.)
Issued 33 years ago (Sept. 1, 1992)
Published 33 years ago (Sept. 1, 1992)
Published Online 20 years, 5 months ago (March 3, 2005)
Published Print 33 years ago (Sept. 1, 1992)
Funders 0

None

@article{SPETH_1992, title={The purification of a detergent‐soluble glucose‐6‐phosphatase from rat liver}, volume={208}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1992.tb17230.x}, DOI={10.1111/j.1432-1033.1992.tb17230.x}, number={3}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={SPETH, Maria and SCHULZE, Hans‐Ulrich}, year={1992}, month=sep, pages={643–650} }