Abstract
Two genetic variants of Xenopus laevis Cu,Zn superoxide dismutase, XSODA and XSODB, have been expressed in Escherichia coli by recombinant DNA techniques. Production of both proteins was obtained, although with different yields, XSODB being more abundant than XSODA in all the conditions tested. Lowering the temperature of growth was found to be a specific factor, decisive in obtaining quantitatively abundant, active Xenopus enzymes. Impaired folding of these proteins in the E.coli cytoplasm was found to parallel their in vitro properties.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cloning, Molecular
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Escherichia coli / genetics
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Gene Expression
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Genetic Variation
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Isoenzymes / chemistry*
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Isoenzymes / genetics
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Isoenzymes / metabolism
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Molecular Weight
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Promoter Regions, Genetic
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Protein Conformation*
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Protein Kinases / genetics
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Superoxide Dismutase / chemistry*
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Superoxide Dismutase / genetics
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Superoxide Dismutase / metabolism
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Thermodynamics
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Xenopus laevis
Substances
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Isoenzymes
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Recombinant Proteins
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Superoxide Dismutase
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Protein Kinases