Applied Biochemistry and Biotechnology

, Volume 16, Issue 1, pp 145–156 | Cite as

Polymeric thiols as enzyme activators of serum creatine phosphokinase

  • Brent A. Burdick
  • Theodore W. Esders
  • James R. Schaeffer
  • Shirley Lynn
Original Article

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.

Index entries

Polymeric thiols polymeric mercaptans creatine phosphokinase solid-phase enzyme activators sulfhydryl-dependent enzymes 

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Copyright information

© Humana Press Inc. 1987

Authors and Affiliations

  • Brent A. Burdick
    • 1
  • Theodore W. Esders
    • 1
  • James R. Schaeffer
    • 1
  • Shirley Lynn
    • 1
  1. 1.Life Sciences Research LaboratoriesEastman Kodak CompanyRochester

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