The complete amino acid sequence of hirudin, a thrombin specific inhibitor: Application of colour carboxymethylation

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 derivat...

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Veröffentlicht in:FEBS letters 1984-01, Vol.165 (2), p.180-184
Hauptverfasser: Dodt, Johannes, Müller, Hans-Peter, Seemüller, Ursula, Chang, Jui-Yoa
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container_title FEBS letters
container_volume 165
creator Dodt, Johannes
Müller, Hans-Peter
Seemüller, Ursula
Chang, Jui-Yoa
description 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.
doi_str_mv 10.1016/0014-5793(84)80165-9
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subjects amino acid sequence
Color carboxymethylation
Hirudin
Hirudo medicinalis
salivary gland
thrombin inhibitor
Tyrosine sulfate
title The complete amino acid sequence of hirudin, a thrombin specific inhibitor: Application of colour carboxymethylation
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