The reaction of chymotrypsin and diisopropylphosphorofluoridate II. The structure of two DP-substituted peptides from chymotrypsin-DP
1. 1. The amino acid sequence of two diisopropylphosphoryl-substituted peptides obtained from α-chymotrypsin-DP by enzyme hydrolysis was established as: glycyl-aspartyl-seryl-glycyl-glycyl-prolyl-leucine and glycyl-aspartyl-seryl-glycyl-glycyl-proline, respectively. 2. 2. The experimental results st...
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Veröffentlicht in: | Biochimica et biophysica acta 1958, Vol.27 (3), p.556-563 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 1.
1. The amino acid sequence of two diisopropylphosphoryl-substituted peptides obtained from α-chymotrypsin-DP by enzyme hydrolysis was established as: glycyl-aspartyl-seryl-glycyl-glycyl-prolyl-leucine and glycyl-aspartyl-seryl-glycyl-glycyl-proline, respectively.
2.
2. The experimental results strongly suggest that the diisopropylphosphoryl group is attached to the hydroxyl group of the seryl residue.
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3. The significance of the investigated peptides in respect to the DFP-binding and ester-splitting ability of α-chymotrypsin is discussed. |
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ISSN: | 0006-3002 1878-2434 |
DOI: | 10.1016/0006-3002(58)90386-X |