Abstract
Commonly observed chemical modifications that occur in proteins during their in vitro purification, storage, and handling are discussed. Covalent modifications described include deamidation and isoaspartate formation, cleavage of peptide bonds at aspartic acid residues, cystine destruction and thiol-disulfide interchange, oxidation of cysteine and methionine residues, and the glycation and carbamylation of amino groups.
MeSH terms
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Aspartic Acid / chemistry
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Aspartic Acid / metabolism
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Cysteine / chemistry
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Cysteine / metabolism
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Cystine / chemistry
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Cystine / metabolism
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Disulfides / chemistry
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Disulfides / metabolism
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Hydrolysis
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Methionine / chemistry
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Methionine / metabolism
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Oxidation-Reduction
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Proteins / chemistry*
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Proteins / metabolism*
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Sulfhydryl Compounds / chemistry
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Sulfhydryl Compounds / metabolism
Substances
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Disulfides
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Proteins
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Sulfhydryl Compounds
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Aspartic Acid
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Cystine
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Methionine
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Cysteine