Purification of five creatine kinase-MM variants from human heart and skeletal muscle

Hemant Vaidya, David N. Dietzler, Joseph F. Leykam, Jack H. Ladenson

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Variants of creatine kinase-MM (variant of ATP:creatine N-phosphotransferase, EC, present in human heart and skeletal muscle, have been purified to homogeneity using DEAE-Sepharose column chromatography and column chromatofocusing techniques. Creatine kinase-MM I-IV were present in both heart and skeletal muscle, while MM-V was found only in heart. The number, ratio and elution profile of the variants during chromatofocusing remained identical even when they purified in the presence of proteinase inhibitors. MM-I-V, on chromatofocusing, were eluted at pH 8.3, 7.9, 7.6, 7.2 and 6.8, respectively. Isoelectric focusing revealed the pI of MM-I-V to be 7.2, 6.9, 6.7, 6.4 and 6.2. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis showed a doublet pattern for creatine kinase-MM variants III-V. However, polyacrylamide gel electrophoresis without SDS indicated homogeneity because each variant showed a single band. The doublet pattern observed in the presence of SDS may reflect the presence of two subunits of slightly different mass.

Original languageEnglish
Pages (from-to)230-237
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number3
StatePublished - Nov 9 1984


  • (Human muscle)
  • Creatine kinase-MM
  • Enzyme variant


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