Isolation and photo-oxidation of lysozyme fragments
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Date
1981
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Abstract
Reduction of the four disulfide bonds and further carboxymethylation of lysozyme followed by its reaction with CNBr brings about L-I, (aa 1 12) and L-II-III (aa 13 129) peptides.
When breaking the polypeptidic chain by CNBr action and freeing the peptides formed through S-S bonds reduction and carboxymethylation three peptides are obtained corresponding to L-I (aa 1 12), L-II (aa 13 105) and L-III (aa 106 129). L-II-III, L-III and L-II peptides were separately subjected to photo-oxidation in presence of riboflavin, in 0.05 M phosphate buffer, pH 7.0. The kinetic analysis of Trp photo-oxidation in L-II-III peptides shows that these residues keep, to a great extent, the degree of exposition they had in native lysozyme. L-II peptide also presents Trp residues with a different degree of exposition. Presence of Tyr photo-oxidation in L-II and L-II-III peptides - what does not take place in native lysozyme - suggests a relationship between photo-oxidation selectivity and the degree of exposition of certain amino acid residues in spatial configuration.Reduction of the four disulfide bonds and further carboxymethylation of lysozyme followed by its reaction with CNBr brings about L-I, (aa 1 12) and L-II-III (aa 13 129) peptides.
When breaking the polypeptidic chain by CNBr action and freeing the peptides formed through S-S bonds reduction and carboxymethylation three peptides are obtained corresponding to L-I (aa 1 12), L-II (aa 13 105) and L-III (aa 106 129). L-II-III, L-III and L-II peptides were separately subjected to photo-oxidation in presence of riboflavin, in 0.05 M phosphate buffer, pH 7.0. The kinetic analysis of Trp photo-oxidation in L-II-III peptides shows that these residues keep, to a great extent, the degree of exposition they had in native lysozyme. L-II peptide also presents Trp residues with a different degree of exposition. Presence of Tyr photo-oxidation in L-II and L-II-III peptides - what does not take place in native lysozyme - suggests a relationship between photo-oxidation selectivity and the degree of exposition of certain amino acid residues in spatial configuration.Reduction of the four disulfide bonds and further carboxymethylation of lysozyme followed by its reaction with CNBr brings about L-I, (aa 1 12) and L-II-III (aa 13 129) peptides.
When breaking the polypeptidic chain by CNBr action and freeing the peptides formed through S-S bonds reduction and carboxymethylation three peptides are obtained corresponding to L-I (aa 1 12), L-II (aa 13 105) and L-III (aa 106 129). L-II-III, L-III and L-II peptides were separately subjected to photo-oxidation in presence of riboflavin, in 0.05 M phosphate buffer, pH 7.0. The kinetic analysis of Trp photo-oxidation in L-II-III peptides shows that these residues keep, to a great extent, the degree of exposition they had in native lysozyme. L-II peptide also presents Trp residues with a different degree of exposition. Presence of Tyr photo-oxidation in L-II and L-II-III peptides - what does not take place in native lysozyme - suggests a relationship between photo-oxidation selectivity and the degree of exposition of certain amino acid residues in spatial configuration.