Complete amino acid sequence of the protease inhibitor from buckwheat seeds
The complete amino acid sequence of protease inhibitor BWI-1 from buckwheat ( Fagopyrum esculentum Moench) seeds has been established by automatic Edman degradation and mass spectrometry. The molecule of the inhibitor consists of 69 amino acid residues, with a molecular mass calculated as 7743.8 Da....
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Veröffentlicht in: | FEBS letters 1995-09, Vol.371 (3), p.264-266 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | The complete amino acid sequence of protease inhibitor BWI-1 from buckwheat (
Fagopyrum esculentum Moench) seeds has been established by automatic Edman degradation and mass spectrometry. The molecule of the inhibitor consists of 69 amino acid residues, with a molecular mass calculated as 7743.8 Da. The active site of the inhibitor containes an Arg
45-Asp
46 bond. Analysis of the amino acid sequence suggests that the buckwheat seed protease inhibitor is a member of the proteinase inhibitor I family. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(95)00899-K |