Polymeric thiols as enzyme activators of serum creatine phosphokinase |
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Authors: | Burdick Brent A Esders Theodore W Schaeffer James R Lynn Shirley |
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Institution: | (1) Life Sciences Research Laboratories, Eastman Kodak Company, 14650 Rochester, NY |
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Abstract: | Several hydrophilic polymeric thiols were prepared from aminoactivated polymeric supports by reaction with N-acetylhomocysteinethiolactone.
Supports include agaroses, cellulose, Glycophase™ controlled-pore glass, and Matrex™ acrylic beads. Thiol content in these
polymers was 3–72 μmol 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. |
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Keywords: | Polymeric thiols polymeric mercaptans creatine phosphokinase solid-phase enzyme activators sulfhydryl-dependent enzymes |
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