Characterization of human carbonic anhydrase III from skeletal muscle

Nicholas Carter, Stephen Jeffery, Alan Shiels, Yvonne Edwards, Terry Tipler, David A. Hopkinson

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A third form of human carbonic anhydrase (CA III), found at high concentrations in skeletal muscle, has been purified and characterized. This isozyme shows relatively poor hydratase and esterase activities compared to the red cell isozymes, CA I and CA II, but is similar to these isozymes in subunit structure (monomer) and molecular size (28,000). CA III is liable to posttranslational modification by thiol group interaction. Monomeric secondary isozymes, sensitive to β-mercaptoethanol, are found in both crude and purified material and can be generated in vitro by the addition of thiol reagents. Active dimeric isozymes, generated apparently by the formation of intermolecular disulfide bridges, also occur but account for only a small proportion of the total protein and appear only when the concentration of CA III is particularly high.

Original languageEnglish
Pages (from-to)837-854
Number of pages18
JournalBiochemical Genetics
Issue number9-10
StatePublished - Oct 1979


  • carbonic anhydrase
  • isozymes
  • muscle


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