Conclusions
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1.
A study was made of the irreversible heat inactivation of free trypsin, and of trypsin in the complex with poly-4(5)-vinylimidazole, in aqueous solution, at pH 6.1, in the temperature range 33–50°.
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2.
The inactivation rate of trypsin decreases in the presence of the polymer, and its activation enthalpy increases when compared with the values of these parameters for free trypsin.
Literature cited
S. V. Kol'tsova, N. G. Illarionova, E. F. Panarin, G. D. Rudkovskaya, and G. V. Samsonov, Izv. Akad. Nauk SSSR, Ser. Khim., 643 (1975).
S. V. Kol'tsova, M. V. Glikina, N. G. Illarionova, and G. S. Samsonov, Mol. Biologiya,5, 225 (1971).
L. Gorini and F. Felix, Biochim. Biophys. Acta,11, 535 (1953).
I. Jon, Biochim. Biophys. Acta,31, 75 (1959).
M. L. Anson and A. E. Mirsky, J. Gen. Physiol,17, 159 (1934).
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Translated from Izvestiya Akademii Nauk SSSR, Seriya Khimicheskaya, No.1, pp.168–171, January, 1976.
We express our gratitude to G. D. Rudkovskaya for graciously supplying the sample of P4VI.
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Kol'tsova, S.V., Samsonov, G.V. Kinetics of heat inactivation of trypsin in complex with poly-4(5)-vinylimidazole. Russ Chem Bull 25, 157–159 (1976). https://doi.org/10.1007/BF00925641
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DOI: https://doi.org/10.1007/BF00925641