Purification and some properties of a major trypsin inhibitor, BTI-I, from broccoli, Brassica oleracea

Purification and some properties of a major trypsin inhibitor, BTI-I, from broccoli, Brassica oleracea

A major trypsin inhibitor (BTI-I) was purified from broccoli, Brassica oleracea, by conventional methods. BTI-I had a molecular weight of 8000 and an isoelectric point of 5.2. BTI-I inhibited bovine and porcine trypsins in an 1:1(M/M) stoichiometry: the approximate Ki's were 6 x 10(-11) M in bo...

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Veröffentlicht in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1995-01, Vol.59 (1), p.117-118
Hauptverfasser: Yoshikawa, H. (Kobe Women's Coll. (Japan)), Kotaru, M, Tanaka, C, Ikeuchi, T
Format: Artikel
Sprache:eng
Schlagworte:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
BRASSICA OLERACEA
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
INHIBIDORES DE ENZIMAS
INHIBITEUR D'ENZYME
PROPIEDADES BIOLOGICAS
PROPRIETE BIOLOGIQUE
PURIFICACION
PURIFICATION
TRIPSINA
TRYPSINE
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Zusammenfassung:A major trypsin inhibitor (BTI-I) was purified from broccoli, Brassica oleracea, by conventional methods. BTI-I had a molecular weight of 8000 and an isoelectric point of 5.2. BTI-I inhibited bovine and porcine trypsins in an 1:1(M/M) stoichiometry: the approximate Ki's were 6 x 10(-11) M in both cases. The chemical modification suggested that BTI-I had an Arg-X bond as a trypsin reactive-site
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.59.117