Amino Acid Sequence of the Protease Inhibitor BWI‐4a From Buckwheat Seeds

The complete amino acid sequence of protease inhibitor BWI‐4a from buckwheat (Fagopyrum esculentum Moench) seeds, consisting of 67 amino acid residues with a single disulfide bond, has been established by Edman degradation in combination with matrix‐assisted laser desorption ionization time‐of‐fligh...

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Veröffentlicht in:IUBMB life 2000-04, Vol.49 (4), p.273-276
Hauptverfasser: Belozersky, Mikhail A., Dunaevsky, Yakov E., Musolyamov, Alexander Kh, Egorov, Tsezi A.
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Sprache:eng
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Zusammenfassung:The complete amino acid sequence of protease inhibitor BWI‐4a from buckwheat (Fagopyrum esculentum Moench) seeds, consisting of 67 amino acid residues with a single disulfide bond, has been established by Edman degradation in combination with matrix‐assisted laser desorption ionization time‐of‐flight mass spectrometry. Its N terminus is blocked by a pyroglutamic acid residue. Mass spectrometric analysis revealed that inhibitor BWI‐4a is present in buckwheat seeds in two isoforms with a single amino acid substitution of Ala40 for Gly40. The reactive site of the inhibitor contains an Arg43‐Asp44 bond. Analysis of the amino acid sequence suggests that the buckwheat seed protease inhibitor is a member of the potato proteinase inhibitor I family.
ISSN:1521-6543
1521-6551
DOI:10.1080/15216540050033122