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 poly...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology 1987-09, Vol.16 (1), p.145-156
Main Authors: BURDICK, B. A, ESDERS, T. W, SCHAEFFER, J. R, LYNN, S
Format: Article
Language:English
Subjects:
3-Mercaptopropionic Acid
Acetylcysteine
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Creatine Kinase - blood
Creatine Kinase - metabolism
Enzyme Activation
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Polyethyleneimine
Polymers
Sulfhydryl Compounds - chemical synthesis
Sulfhydryl Compounds - pharmacology
Thiophenes
Transferases
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Summary: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.
ISSN:0273-2289
1559-0291
DOI:10.1007/BF02798363