Is thermostability of glucose‐6‐phosphatase indeed dependent on a stabilizing protein?

FEBS Letters

Schulze, Hans-Ulrich¹  Speth, Maria¹ 

[1] Biochemisches Institut der Justus Liebig Universitat Giessen, Friedrichstrasse 24, 6300 Giessen, FRG

关键词: Glucose-6-phosphatase enzyme purification (Rat liver) Microsomal membrane Thermostability Stabilizing protein;   

DOI  :  10.1016/0014-5793(86)80643-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Partial purification of glucose-6-phosphatase from rat liver microsomes by solubilization of the membranes with the non-ionic detergent Triton X-144 at pH 6.5 and the removal of inactivating detergent by hydrophobic chromatography results in a thermostable enzyme protein which is not dependent on stabilizing phospholipids or proteins. The readdition of low amounts of detergent immediately causes a conversion into a thermo-unstable phosphodydrolase protein. Thus these findings present evidence that heatinstability of partially purified glucose-6-phosphatase derives from traces of inactivating detergent changing the structural properties of the phosphohydrolase rather than from the absence of the postulated specific stabilizing protein.

【 授权许可】

Unknown