Covalent binding of human serum albumin and ovalbumin by chloramine-T and chemical modification of the proteins |
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Authors: | Jeffrey C Evans Simon K Jackson Christopher C Rowlands Martin D Barratt |
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Institution: | Chemistry Department, University of College, Cardiff Great Britain;Environment Safety Laboratory, Unilever Research, Colworth House, Shambrook, Bedfore Great Britain |
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Abstract: | The covalent binding of 35S-chloramine-T to human resum albumin (HSA) and ovalbumin is described. At pH 6.5, up to 24 chloramine-T molecules were found to be covalently bound per molecule of HSA; with ovalbumin the binding was only 5–7 molecule per protein molecule. Binding was accompanied by extensive modification of methionine, cysteine, histidine, tyrosine and lysine. Three new peaks appeared in the amino acid profiles of the modified proteins; two were identified as 1-aminoadipic acid (oxidation of lysine) and 3-chlorotyrosine. The most sites for covalent binding are lysine residues. |
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