A polymer regulator of enzyme activity |
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Authors: | I. L. Valuev I. V. Obydennova L. V. Vanchugova L. I. Valuev N. A. Sivov T. A. Valueva |
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Affiliation: | 1.Topchiev Institute of Petrochemical Synthesis,Russian Academy of Sciences,Moscow,Russia;2.Federal Research Centre Fundamentals of Biotechnology,Russian Academy of Sciences (Bach Institute of Biochemistry, Russian Academy of Sciences),Moscow,Russia |
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Abstract: | The reaction of the amino group of α-chymotrypsin with poly(N,N-diethylacrylamides) bearing terminal carboxyl groups which have the degree of polymerization ranging from 30 to 180 and which possess an LCST of 34–29°C affords polymer derivatives of the enzyme. It is found that, upon an increase in the temperature of the aqueous solution of the resulting derivatives to 40°C, the derivative with a degree of polymerization of 180 precipitates at 34°C, while the derivatives with a degree of polymerization of 30–80 remain in solution. The activity of α-chymotrypsin as a part of the derivatives with a degree of polymerization of 30 does not change with increasing temperature, whereas the activity of the enzyme as a part of the derivatives with degrees of polymerization of 60 and 80 decays almost to zero near the LCST of the initial polymers. Such a change in the enzyme activity is reversible (the activity fully recovers with a decrease in temperature). |
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