Triglyceride, diglyceride, monoglyceride, and cholesterol ester hydrolases in chicken adipose tissue activated by adenosine 3':5'-Monophosphate-dependent protein kinase. Chromatographic resolution and immunochemical differentiation from lipoprotein lipase.

摘要: Abstract Hormone-sensitive lipase and cholesterol ester hydrolase of chicken adipose tissue were markedly activated by adenosine 3':5'-monophosphate (cAMP)-dependent protein kinase (on the average, 235 to 275%; occasionally as much 1000%). Diglyceride monoglyceride hydrolases also activated, but a lesser extent (60 87%). The activation all four was inhibited inhibitor reversed addition exogenous kinase. Following cAMP-dependent kinase, deactivated in Mg2+-dependent reaction then reactivated or near initial levels on incubation with cAMP Mg2+-ATP. reversible deactivation is assumed reflect activity one more phosphatases. maximum obtainable for decreased when had been previously exposed glucagon, indicating that glucagon-induced probably similar identical demonstrated cell-free preparations. pH optima activities (7.13 7.38). Although absolute relative degrees differed according particular emulsified substrates used, results do not rule out possibility are referable single hormone-sensitive hydrolase. acyl separated from lipoprotein heparin-Sepharose affinity chromatography. Lipoprotein active against triolein, diolein, monoolein, oleate. Incubation cAMP, Mg2+ATP no effect any three activities. further purified homogeneity used prepare antiserum rabbits. immunoglobin G fraction these antisera completely eluted columns. However, (not retained chromatography) anti-lipoprotein G, anti-lopoprotein did affect process crude fractions. Thus, lipase, functionally distinct enzymes, have physically resolved immunochemically distinguished. Apparently regulated, at least directly,