Title : Identification of photooxidation sites in bovine alpha-crystallin.

Pub. Date : 1997 Nov

PMID : 9383987






2 Functional Relationships(s)
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1 Tryptophan fluorescence decreased exponentially with increasing time of UV exposure and peptides containing residues 1-11 of alpha A-crystallin and 1-11, 12-22 and 57-69 of alpha B-crystallin were determined to be oxidized by shifts of 16 D or multiples of 16 Da above the mass of the unmodified peptide. Tryptophan crystallin alpha B Bos taurus
2 The specific sites of photooxidation indicate that the N-terminal regions of alpha A- and alpha B-crystallin are exposed to an aqueous environment and are in the vicinity of tryptophan residues from neighboring subunits. Tryptophan crystallin alpha B Bos taurus