The separation and properties of phosphoprotein phosphatase modulators from brown adipose tissue of young rats and the changes in their concentration during development.

Abstract

The heat-stable modulators of phosphoprotein phosphatase activity have been partically purified from brown adipose tissue. A nonphosphorylatable inhibitor of phosphorylase phosphatase (inhibitor 2) and an activator of phosphohistone phosphatase were similar to the corresponding modulators from muscle and liver in both their physical properties and in their relative effects upon three different preparations of phosphatase. An inhibitor of phosphorylase phosphatase that was only active when phosphorylated was eluted from DEAE-cellulose by 80 mM NaCl (inhibitor 1'). Only a small amount of inhibitor was eluted at 20 mM NaCl (inhibitor 1), which is the concentration that eluted the bulk of the phosphorylatable inhibitor in muscle and liver. Inhibitor 1 and inhibitor 1' had similar physical properties but differed in their activities towards the different phosphatases. It is suggested that they are different forms of the same protein and that inhibitor 1' more closely resembles the native inhibitor. The modulators did not compete with each other and were probably not subunits of a phosphatase complex. However, the direction and timing of the changes in their concentration in brown fat during the developmental period indicate that the inhibitors, at least, perform some useful physiological function in the tissue. The concentration of inhibitor 2 was high before birth and for 10 days after birth, when the tissue was proliferating. The concentration of the phosphorylatable inhibitor was highest immediately after birth and for the next 16 days, which is the period of greatest thermogenic activity of brown fat.