Polymeric thiols as enzyme activators of serum creatine phosphokinase.
Several hydrophilic polymeric thiols were prepared from amino-activated polymeric supports by reaction with N-acetylhomocystein ethiolactone. Supports include agaroses, cellulose, Glycophase controlled-pore glass, and Matrex acrylic beads. Thiol content in these polymers was 3-72 mumol SH/g dry polymer. Several were effective solid-phase activators of the sulfhydryl-dependent enzyme creatine phosphokinase at concentrations comparable to that of monomeric thiol required for enzyme activation. The kinetic activation curves for the polymeric and the monomeric (thioglucose) activators were similar, suggesting unhindered interaction of the enzyme with the polymeric activator.
D015097:3-Mercaptopropionic Acid; D000111:Acetylcysteine; D003402:Creatine Kinase / Q000097:blood / Q000378:metabolism*; D004789:Enzyme Activation; D011094:Polyethyleneimine; D011108:Polymers; D013438:Sulfhydryl Compounds / Q000138:chemical synthesis / Q000494:pharmacology*; D013876:Thiophenes
D011108:Polymers; D013438:Sulfhydryl Compounds; D013876:Thiophenes; C000486:citiolone; D011094:Polyethyleneimine; D015097:3-Mercaptopropionic Acid; D003402:Creatine Kinase; D000111:Acetylcysteine