erythro-beta-Hydroxyaspartic acid in bovine factor IX and factor X.
To localize beta-hydroxyaspartic acid in factor IX and factor X the two proteins were cleaved with cyanogen bromide and trypsin, respectively. Peptides containing beta-hydroxyaspartic acid were isolated and subjected to Edman degradation. The phenylthiohydantoin derivative of beta-hydroxyaspartic acid was identified by HPLC in position 3 in the factor IX fragment and in position 1 in the factor X fragment. This corresponds to position 64 in factor IX and position 63 in the light chain of factor X. The assignments were confirmed by subtractive Edman degradation and with the dansyl method.
D000595:Amino Acid Sequence; D000818:Animals; D001224:Aspartic Acid / Q000031:analogs & derivatives / Q000032:analysis; D002417:Cattle; D003488:Cyanogen Bromide; D005164:Factor IX / Q000032:analysis*; D005170:Factor X / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D010669:Phenylthiohydantoin; D011499:Protein Processing, Post-Translational; D014357:Trypsin
D010446:Peptide Fragments; C011274:3-hydroxyaspartic acid; D010669:Phenylthiohydantoin; D001224:Aspartic Acid; D005164:Factor IX; D005170:Factor X; D014357:Trypsin; D003488:Cyanogen Bromide