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Is thermostability of glucose‐6‐phosphatase indeed dependent on a stabilizing protein?
Author(s) -
Speth Maria,
Schulze Hans-Ulrich
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80643-3
Subject(s) - thermostability , chemistry , phosphatase , biochemistry , biophysics , enzyme , biology
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.