Cyclic GMP and cyclic GMP-dependent protein kinase in brown adipose tissue of developing rats

1979 ◽  
Vol 582 (1) ◽  
pp. 122-131 ◽  
Author(s):  
J SKALA ◽  
B KNIGHT
Keyword(s):  
Adipose Tissue ◽  
Protein Kinase ◽  
Brown Adipose Tissue ◽  
Cyclic Gmp ◽  
Dependent Protein Kinase ◽  
Brown Adipose ◽  
Dependent Protein

scholarly journals Adipose-tissue phosphofructokinase. Rapid purification and regulation by phosphorylation in vitro

1985 ◽  
Vol 232 (3) ◽  
pp. 897-904 ◽  
Author(s):  
E M Sale ◽  
R M Denton
Keyword(s):  
Adipose Tissue ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Single Step ◽  
Optimal Conditions ◽  
Dependent Protein Kinase ◽  
Brown Adipose ◽  
Dependent Protein ◽  
Rapid Purification

A new procedure for the purification of phosphofructokinase using Blue Dextran-Sepharose is described. This allowed an approx. 1000-fold purification of phosphofructokinase from rat white and brown adipose tissue to be achieved in essentially a single step. The purified enzymes from both tissues were found to exhibit hyperbolic kinetics with fructose 6-phosphate, to be inhibited by ATP and citrate, and to be activated by 5′-AMP, phosphate and fructose 2,6-bisphosphate. The enzymes were phosphorylated by the catalytic subunit of cyclic AMP-dependent protein kinase, and phosphorylation was found to be associated with increases in activity when the enzymes were assayed under appropriate sub-optimal conditions. In particular, the phosphorylated enzymes exhibited less inhibition by ATP and the white-adipose-tissue enzyme was more sensitive to activation by fructose 2,6-bisphosphate. It is suggested that an increase in the cytoplasmic concentration of cyclic AMP in tissues other than liver may result in an increase in glycolysis through the phosphorylation of phosphofructokinase by cyclic AMP-dependent protein kinase.

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