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- W2076264247 abstract "Abstract Two inhibitors of Aedes aegypti trypsin have been purified from bovine serum and characterized. Inhibitor I has a molecular weight of about 43,500 and inhibitor II has a very high molecular weight (possibly about 1,000,000). They are located electrophoretically in association with the α1- and the α2-globulin fractions of serum respectively. Stoichiometric measurements indicate that the molar ratios of trypsin-inhibitor I and trypsin-inhibitor II complexes are 3.5 and 1.7 respectively. The Hill plot indicates that 2 molecules of inhibitor (inhibitor I or inhibitor II) inactivate 1 enzymic site of trypsin. In vitro, the formation of trypsin-inhibitor II complex has been demonstrated by Sephadex gel filtration and cellulose acetate electrophoresis. The complex retains most of its esterolytic activity but has a very low proteolytic activity. The esterolytic activity of the trypsin-inhibitor II complex is not inhibited by inhibitor I, soybean trypsin inhibitor, or phenylmethanesulphonyl fluoride (PMSF). The free trypsin esterolytic activity is inhibited by these substances. The complex has a lower Km than the free trypsin, but both have a similar pH optimum. Inhibitors I and II competitively inhibit the tryptic hydrolysis of denatured bovine haemoglobin. These two inhibitors and whole bovine serum non-competitively inhibit the tryptic hydrolysis of α-N- Benzoyl- dl -arginine -p- nitroanilide HCl (BAPNA) at 37°C. The mechanism of trypsin inhibition has been discussed from the aspect of the types of inhibition, and the thermo-dynamic parameters of the enzyme-inhibitor and the enzyme-substrate complexes." @default.
- W2076264247 created "2016-06-24" @default.
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- W2076264247 date "1971-06-01" @default.
- W2076264247 modified "2023-09-27" @default.
- W2076264247 title "The interactions of Aedes aegypti (L.) trypsin with its two inhibitors found in bovine serum" @default.
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- W2076264247 doi "https://doi.org/10.1016/0020-1790(71)90074-6" @default.
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