## Abstract It was previously demonstrated that some plant inhibitors are able to inactivate the bacterial proteinase subtilisin; since information concerning the effect of plant inhibitors on other microbial proteinases remains limited, we decided to determine the activity of the soybean Kunitz an
Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch
β Scribed by Nathalia I. Larionova; Stepan S. Vartanov; Nadezhda V. Sorokina; Inna P. Gladysheva; Sergey D. Varfolomeyev
- Publisher
- Springer-Verlag
- Year
- 1997
- Tongue
- English
- Weight
- 411 KB
- Volume
- 62
- Category
- Article
- ISSN
- 0273-2289
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## Abstract The effect of pH and temperature on the apparent association equilibrium constant (__K__~a~) for the binding of the soybean BowmanβBirk proteinase inhibitor (BBI) and of its chymotrypsin and trypsin inhibiting fragments (FβC(p), FβT(p) and FβT(t), respectively) to bovine Ξ±βchymotrypsin
## Background: Bowman birk inhibitor (bbi) is an anticarcinogenic serine protease inhibitor that may inhibit the protease activity of prostate-specific antigen (psa) and the growth of human prostate cancer xenografts in nude mice. ## Methods: Human prostate cancer xenografts were established by i
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