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Trypsin inhibitors of broad bean (Vicia faba L.)

Abstract

We have isolated and purified two trypsin inhibitors from broad bean(Vicia faba L.). On the evidence of acrylamide gel electrophoresis these two inhibitors, labelled BBTI-1 and BBTI-2, are pure and distinct. Trypsin inactivation and stability studies indicate that BBTI-2 has the greater specific activity and is the more heat stable than BBTI-1. The amino acid pattern confirms the distinctness of the two inhibitors. From qualitative evidence it is inferred that two inhibitors are not simple proteins, but possibly glycoproteins which could explain the stability characteristics observed.

Zusammenfassung

Wir haben aus Dicken Bohnen(Vicia faba) zwei Trypsin-Inhibitoren isoliert und gereinigt. Nach den Befunden der Acrylamidgel-Elektrophorese sind diese beiden Inhibitoren, mit den Bezeichnungen BBTI-1 und BBTI-2, rein und von einander verschieden. Trypsin-Inaktivierungs- und Stabilisierungs-Versuche ergaben, daß BBTI-2 eine größere spezifische Aktivität besitzt und hitzestabiler ist als BBTI-1. Die Aminosäurenzusammensetzung bestätigt die Verschiedenheit der beiden Inhibitoren. Aus den qualitativen Befunden kann gefolgert werden, daß zwei Inhibitoren nicht einfache Proteine sind, aber möglicherweise Glycoproteine, die den beobachteten stabilen Charakter erklären würden.

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Warsy, A.S., Stein, M. Trypsin inhibitors of broad bean (Vicia faba L.). Plant Food Hum Nutr 23, 157–169 (1973). https://doi.org/10.1007/BF01092249

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Keywords

  • Acrylamide
  • Trypsin Inhibitor
  • Stability Characteristic
  • Broad Bean
  • Qualitative Evidence