The complete amino acid sequence of hirudin,a thrombin specific inhibitor: Application of colour carboxymethylation |
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Authors: | Johannes Dodt Hans-Peter Müller Ursula Seemüller Jui-Yoa Chang |
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Institution: | 1. Department of Clinical Chemistry and Clinical Biochemistry, University of Munich, Munich, Switzerland;2. Plantorgan Werk KG, Bad Zwischenahn, FRG;3. Pharmaceuticals Research Laboratories, CIBA-GEIGY Ltd, Basel, Switzerland |
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Abstract: | Color carboxymethylation of cysteine residues with a new chromophoric reagent dimethylaminoazobenzene iodoacetamide, was applied to the micro-sequence analysis of hirudin, a thrombin specific inhibitor. Six cysteine residues of the reduced hirudin were detected as colored phenylthiohydantoin derivative and 3 tryptic peptides of hirudin (all containing cysteines) were isolated as colored peptide. The complete hirudin sequence, including 6 uncertain positions left in the previous report Petersen T.E. (1976) in: Protides of the Biological Fluids; 23rd Colloquium, pp. 145, Pergamon Press, London] was established. |
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Keywords: | Hirudin Tyrosine sulfate Color carboxymethylation DABIA 4-dimethylaminobenzene 4-iodoacetamide DABITC dimethylaminoazobenzene isothiocyanate DABS-Cl dimethylaminoazobenzene sulfonyl chloride HPLC high-performance liquid chromatography PTH phenylthiohydantoin |
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