Cleavage of human serum transferrin with N-bromosuccinimide.
Human serum transferrin was fragmented by N-bromosuccinimide and reduction-alkylation. It was observed that there were at least two each of tryptophanyl-serine and tryptophanyl-aspartic acid, and one each of tryptophanyl-alanine and tryptophanyl-glutamic acid bonds. The size of fragments detected by polyacrylamide gel electrophoresis ranged from 8,000 to 70,000 daltons. Several of the fragments were isolated in a homogeneous form with respect to molecular weight, but were shown to be mixtures of at least five molecular species each by end group analysis.
D000409:Alanine / Q000032:analysis; D001224:Aspartic Acid / Q000032:analysis; D001974:Bromosuccinimide; D004591:Electrophoresis, Polyacrylamide Gel; D005973:Glutamine / Q000032:analysis; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding / Q000187:drug effects; D013388:Succinimides; D014168:Transferrin / Q000032:analysis; D014364:Tryptophan / Q000032:analysis
D010446:Peptide Fragments; D013388:Succinimides; D014168:Transferrin; D005973:Glutamine; D001224:Aspartic Acid; D014364:Tryptophan; D001974:Bromosuccinimide; D000409:Alanine