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High activity of NADP-dependent malic enzyme in mitochondria from abdomen muscle of the crayfish Orconectes limosus.
Metadata
JournalComp. Biochem. Physiol., BNot FoundDate
1977
Type
Research Support, Non-U.S. Gov't
Journal Article
Volume
1977 / 58 : 297-301
Author
Skorkowski EF 1, Swierczyński J , Aleksandrowicz Z
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Doi
PMIDMESH
Abdominal Muscles
Animals
Astacoidea
Hydrogen-Ion Concentration
Malate Dehydrogenase
Malate Dehydrogenase (NADP+)
Mitochondria
Pyruvates
Abstract
1. Mitochondria isolated from abdomen muscle of crayfish Orconectes limosus exhibit malic enzyme activity in the presence of L-malate, NADP and Mn2+ ions after addition of Triton X-100. Under optimal conditions about 230 nmole of reduced NADP and an equivalent amount of pyruvate are produced per min per mg of mitochondrial protein. 2. The pH optimum for decarboxylation of L-malate is about 7.5. 3. The apparent Km for L-malate, NADP and Mn2+ ions was found to be 0.66, 0.012, and 0.0025 mM, respectively. 4. The requirement for Mn2+ can be replaced by Mg2+, Co2+ and Ni2+ ions; however, higher concentrations of these ions than Mn2+ are required for a full stimulation of malic enzyme activity. 5. Oxaloacetate and pyruvate inhibited the enzyme activity in a competitive manner with apparent Ki values of 0.05 mM and 5.4 mM, respectively.
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Comp. Biochem. Physiol., BComparative biochemistry and physiology. B, Comparative biochemistry
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