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Limited proteolysis of chloroplast fructose 1,6-bisphosphatase by subtilisin

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
97
Issue
4
Identifiers
DOI: 10.1016/s0006-291x(80)80008-8
Disciplines
  • Biology

Abstract

Summary Treatment of spinach chloroplast fructose 1,6-bisphosphatase with subtilisin results in a partial loss of enzyme activity measured at pH 8.3 as the consequence of a shift of the pH optimum of the enzyme to a more alkaline pH. The subtilisin-treated enzyme remains tetrameric, but sodium dodecyl-sulfate polyacrylamide gel electrophoresis reveals that the native 44,000 molecular weight subunit is converted to a species of 40,000 molecular weight. Thus, although choloroplast fructose 1,6-bisphosphatase is considered to be an enzyme very distinct from gluconeogenic fructose 1,6-bisphosphatases these results show a resemblance in their behavior towards subtilisin.

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