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The complete amino acid sequence of hirudin, a thrombin specific inhibitor
Author(s) -
Dodt Johannes,
Müller Hans-Peter,
Seemüller Ursula,
Chang Jui-Yoa
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80165-9
Subject(s) - hirudin , iodoacetamide , chemistry , cysteine , thrombin , peptide , sequence (biology) , biochemistry , peptide sequence , reagent , stereochemistry , organic chemistry , biology , enzyme , gene , immunology , platelet
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.