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Characterization of human carbonic anhydrase III from skeletal muscle

✍ Scribed by Nicholas Carter; Stephen Jeffery; Alan Shiels; Yvonne Edwards; Terry Tipler; David A. Hopkinson

Publisher: Springer
Year: 1979
Tongue: English
Weight: 828 KB
Volume: 17
Category: Article
ISSN: 0006-2928
DOI: 10.1007/bf00504307

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✦ Synopsis

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 beta-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.

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