Comparison of purified bovine heart and rat liver 6-phosphofructo-2-kinase. Evidence for distinct isoenzymes

1 October 1985

journal article
research article
Published by Portland Press Ltd. in Biochemical Journal

Vol. 231 (1) , 193-196
https://doi.org/10.1042/bj2310193

Abstract

Rat liver and bovine heart 6-phosphofructo-2-kinase were purified by the same procedure. Compared with the liver enzyme, the heart enzyme had a smaller apparent Mr, different kinetic properties, was not inactivated by cyclic AMP-dependent protein kinase, and contained less fructose-2,6-bisphosphatase activity. These differences suggest that heart and liver 6-phosphofructo-2-kinase are distinct isoenzymes. Likewise, 6-phosphofructo-2-kinase from rat heart and skeletal muscle was not inactivated on treatment with cyclic AMP-dependent protein kinase.

This publication has 20 references indexed in Scilit:

Activation of rat heart phosphofructokinase‐2 by insulin in vivo
FEBS Letters, 1984
GLUCONEOGENESIS AND RELATED ASPECTS OF GLYCOLYSIS
Annual Review of Biochemistry, 1983
[6] Catalytic subunit of cAMP-dependent protein kinase
Published by Elsevier ,1983
[1] Assays of protein kinase
Published by Elsevier ,1983
The glycolytic cascade in pancreatic islets
Diabetologia, 1982
Fructose‐2,6‐bisphosphatase from Rat Liver
European Journal of Biochemistry, 1982
The tissue distribution of fructose-2,6-P2 and fructose-6-P,2-kinase in rats and the effect of starvation diabetes and hypoglycemia on hepatic fructose-2,6-P2 and fructose-6-P,2-kinase
Biochemical and Biophysical Research Communications, 1982
Trace polypeptides in cellular extracts and human body fluids detected by two-dimensional electrophoresis and a highly sensitive silver stain.
Proceedings of the National Academy of Sciences, 1979
A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
Analytical Biochemistry, 1976
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Nature, 1970