Inhibition of rabbit skeletal muscle phosphorylase phosphatase by spermine.
The effect of three naturally occurring polyamines (putrescine, spermidine, and spermine) on the activity of rabbit skeletal muscle phosphorylase phosphatase was investigated. Only spermine significantly inhibited the enzyme. The mode of inhibition (ki value of 0.3 mM) of the phosphatase by spermine appears to be different from that caused by divalent metal ions or by other organic cations, such as arginine and lysine esters, since it is noncompetitive with respect to the substrate, phosphorylase a.
D000818:Animals; D004305:Dose-Response Relationship, Drug; D007700:Kinetics; D009132:Muscles / Q000187:drug effects / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors*; D010765:Phosphorylase Phosphatase / Q000037:antagonists & inhibitors*; D011700:Putrescine / Q000494:pharmacology; D011817:Rabbits; D013095:Spermidine / Q000494:pharmacology; D013096:Spermine / Q000494:pharmacology*
D013096:Spermine; D010765:Phosphorylase Phosphatase; D010744:Phosphoric Monoester Hydrolases; D013095:Spermidine; D011700:Putrescine