erythro‐β‐hydroxyaspartic acid in bovine factor IX and factor X
Copyright policy )erythro‐β‐hydroxyaspartic acid in bovine factor IX and factor X
To localize β‐hydroxyaspartic acid in factor IX and factor X the two proteins were cleaved with cyanogen bromide and trypsin, respectively. Peptides containing β‐hydroxyaspartic acid were isolated and subjected to Edman degradation. The phenylthiohydantoin derivative of β‐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.
- Lund University Sweden
Aspartic Acid, Blood coagulation, Peptide Fragments, Factor IX, β-Hydroxyaspartic acid, Factor X, Phenylthiohydantoin, Animals, Cattle, Trypsin, Posttranslational modification, Amino Acid Sequence, Cyanogen Bromide, Vitamin K-dependent protein, Protein Processing, Post-Translational
Aspartic Acid, Blood coagulation, Peptide Fragments, Factor IX, β-Hydroxyaspartic acid, Factor X, Phenylthiohydantoin, Animals, Cattle, Trypsin, Posttranslational modification, Amino Acid Sequence, Cyanogen Bromide, Vitamin K-dependent protein, Protein Processing, Post-Translational
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