MedicGo
Carp (Cyprinus carpio) muscle fructose 1,6-bisphosphatase: purification and some properties.
Metadata
JournalComp. Biochem. Physiol., BNot FoundDate
1977
Type
Research Support, Non-U.S. Gov't
Journal Article
Volume
1977 / 58 : 291-5
Author
Rosenmann E 1, González AM , Hein S , Marcus F
Affiliation

No Data

Doi
PMIDMESH
Adenosine Monophosphate
Animals
Carps
Cations
Cyprinidae
Fructose-Bisphosphatase
Hydrogen-Ion Concentration
Molecular Weight
Muscles
Rabbits
Abstract
1. Fructose 1,6-bisphosphatase from the white muscle tissue of the carp, Cyprinus carpio L. was purified. 2. The mol. wt of the enzyme was 145,000. Its subunit mol. wt was ca. 35,000. 3. The enzyme exhibited neutral pH optimum, activation by monovalent cations, and temperature-dependent allosteric AMP inhibition. 4. Carp muscle fructose 1,6-bisphosphatase was 10- to 30-fold more sensitive to AMP inhibition than the carp liver enzyme. 5. The carp muscle enzyme was less sensitive to AMP inhibition than the muscle enzyme from a homeothermic mammal. These results are interpreted as an example of temperature-adaptation of an enzyme regulatory property.
Fav
Like
Download
Share
Export
Cite
C
Comp. Biochem. Physiol., BComparative biochemistry and physiology. B, Comparative biochemistry
Metadata
Location
From

No Data

© 2017 - 2020 Medicgo
Powered by some medical students