Partial non-cleavage by cyanogen bromide of a methionine--cystine bond from human serum albumin and bovine alpha-lactalbumin.
When human albumin was treated with CNBr, a fragment designated D was obtained and attributed to the absence from some of the albumin molecules of methionine at position 123 [Lapresle & Doyen (1975) Biochem. J. 151, 637-643]. The present study shows that methionine-123 is converted into homoserine without cleavage of the subsequent methionine-cystine bond. With bovine alpha-lactalbumin, a further example of non-cleavage of a methionine-cystine bond with conversion of methionine into homoserine is reported.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003488:Cyanogen Bromide; D003553:Cystine; D006801:Humans; D007768:Lactalbumin; D008715:Methionine; D010446:Peptide Fragments / Q000032:analysis; D012709:Serum Albumin
D000596:Amino Acids; D010446:Peptide Fragments; D012709:Serum Albumin; D003553:Cystine; D007768:Lactalbumin; D008715:Methionine; D003488:Cyanogen Bromide