Characterization of human carbonic anhydrase III from skeletal muscle

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...

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Bibliographic Details
Published in:Biochemical genetics 1979-10, Vol.17 (9-10), p.837-854
Main Authors: Carter, N, Jeffery, S, Shiels, A, Edwards, Y, Tipler, T, Hopkinson, D A
Format: Article
Language:English
Subjects:
Adult
Amino Acids - analysis
Carbonic Anhydrases - analysis
Carbonic Anhydrases - isolation & purification
Carbonic Anhydrases - metabolism
Electrophoresis, Polyacrylamide Gel
Electrophoresis, Starch Gel
Erythrocytes - enzymology
Humans
Infant, Newborn
Isoelectric Focusing
Isoenzymes - metabolism
Molecular Weight
Muscles - enzymology
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Summary: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.
ISSN:0006-2928
1573-4927
DOI:10.1007/BF00504307