Zhurnal Prikladnoii Spektroskopii
Žurnal prikladnoj spektroskopii

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DETERMINATION OF RATES OF α-CHYMOTRYPSIN-CATALYZED REACTIONS АT DIFFERENT TEMPERATURES AND pH BY RAMAN SPECTROSCOPY

I. A. Balakhnina, N. N. Brandt, A. A. Mankova, A. Yu. Chikishev, I. G. Shpachenko

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Abstract

Spontaneous Raman spectroscopy is used to determine rates of an enzymatic reaction. Time dependences of integral Raman intensities in the spectra of reaction mixtures are analyzed. The rates of α-chymotrypsin-catalyzed reaction are determined at different temperatures and pH values.

Keywords

Raman spectroscopy, enzymatic reaction rate, enzyme kinetics, activity

About the Authors

I. A. Balakhnina

Lomonosov Moscow State University
Russian Federation
Moscow, 119991

N. N. Brandt

Lomonosov Moscow State University
Russian Federation
Moscow, 119991

A. A. Mankova

Lomonosov Moscow State University
Russian Federation
Moscow, 119991

A. Yu. Chikishev

Lomonosov Moscow State University
Russian Federation
Moscow, 119991

I. G. Shpachenko

Lomonosov Moscow State University
Russian Federation
Moscow, 119991

References

1. H. Bisswanger. Enzyme Kinetics: Principles and Methods, Germany, Wiley-VCH Verlag GmbH & Co (2017)

2. H. Bisswanger. Perspectives in Science, 1 (2014) 41—55

3. D. L. Purich. Enzyme Kinetics: Catalysis & Control, Boston, Elsevier (2010)

4. H. U. Bergmeyer. Methods of Enzymatic Analysis, USA, Academic Press (1974)

5. J. Cielecka-Piontek. Appl. Spectrosc., 67, N 7 (2013) 703—708

6. F. Mirazizi, A. Bahrami, K. Haghbeen, H. Shahbani Zahiri, M. Bakavoli, R. L. Legge. J. Enzyme Inhib. Med. Chem., 31, N 6 (2016) 1162—1169

7. B. Tang, F. Han, L. Ma. Chin. J. Anal. Chem., 29, N 3 (2001) 347—354

8. U. Kettling, A. Koltermann, P. Schwille, M. Eigen. Proc. Natl. Acad. Sci. USA, 95, N 4 (1998) 1416—1420

9. Y. C. Tsai, Z. Jin, K. A. Johnson. Anal. Biochem., 384, N 1 (2009) 136—144

10. E. Navarro-Perán, J. Cabezas-Herrera, A. N. P. Hiner, T. Sadunishvili, F. García-Cánovas, J. N. Rodríguez-López. Biochemistry, 44, N 20 (2005) 7512—7525

11. T. K. Harris, M. M. Keshwani. Guide to Protein Purification, Methods in Enzymology Eds. R. R. Burgess, M. P. Deutscher, 463, Academic Press, USA (2009) 57—71

12. C. Aguirre, I. Condado-Morales, L. F. Olguin, M. Costas. Anal. Biochem., 479, N 15 (2015) 18—27

13. M. Noda, Y. Matoba, T. Kumagai, M. Sugiyama. Biochem. J., 389 (2005) 491—496

14. F. Zsila. J. Phys. Chem. B, 117, N 37 (2013) 10798—10806

15. И. А. Балахнина, Н. Н. Брандт, А. А. Манькова, А. Ю. Чикишев, И. Г. Шпаченко. Журн. прикл. спектр., 84, № 4 (2017) 628—634 [I. A. Balakhnina, N. N. Brandt, A. A. Mankova, A. Yu. Chikishev, I. G. Shpachenko. J. Appl. Spectr., 84, N 4 (2017) 650—656]

16. И. Г. Шпаченко, Н. Н. Брандт, А. Ю. Чикишев. Вестн. МГУ. Физика. Астрономия, № 6 (2018) 67—73 [I. G. Shpachenko, N. N. Brandt, A. Yu. Chikishev. Mosc. Univ. Phys. Bull., 73, N 6 (2018) 644—650]

17. N. Brun, I. Youssef, M.-C. Chevrel, D. Chapron, C. Schrauwen, S. Hoppe, P. Bourson, A. Durand. J. Raman Spectrosc., 44, N 6 (2013) 909—915

18. I. Csontos, H. Pataki, A. Farkas, H. Bata, B. Vajna, Z. K. Nagy, G. Keglevich, G. J. Marosi. Org. Process Res. Dev., 19, N 1 (2015) 189—195

19. D. Šahnić, E. Meštrović, T. Jednačak, I. Habinovec, J. Parlov Vuković, P. Novak. Org. Process Res. Dev., 20, N 12 (2016) 2092—2099

20. M. Assirelli, W. Xu, W. Chew. Org. Process Res. Dev., 15, N 3 (2011) 610—621

21. Y. Ou, R. E. Wilson, S. G. Weber. Annu. Rev. Anal. Chem., 11, N 1 (2018) 509—533

22. I. A. Balakhnina, N. N. Brandt, A. Yu. Chikishev, A. A. Mankova, I. G. Shpachenko. Vib. Spectrosc., 106 (2020) 103004

23. F. J. Kezdy, M. L. Bender. Biochemistry, 1, N 6 (1962) 1097—1106

24. M. L. Bender, F. J. Kezdy, F. C. Wedler. J. Chem. Educ., 44, N 2 (1967) 84—88

25. S. Z. Vatsadze, A. V. Medved’ko, S. A. Kurseev, O. I. Pokrovskiy, O. O. Parenago, M. O. Kostenko, I. V. Ananyev, K. A. Lyssenko, D. A. Lemenovsky, G. M. Kazankov, V. V. Lunin. Organometallics, 36 (2017) 3068—3075

26. S. Vatsadze, A. Medved'ko, G. Kazankov, S. Kurzeev. ChemSpider SyntheticPages, 705, http://cssp.chemspider.com

27. N. N. Brandt, A. Yu. Chikishev. Laser. Phys., 12 (2002) 647—652

28. N. N. Brandt, A. Yu. Chikishev, A. I. Sotnikov, Yu. A. Savochkina, I. I. Agapov, A. G. Tonevitsky. J. Mol. Struct., 735-736 (2005) 293—298

29. N. N. Brandt, A. Yu. Chikishev, V. N. Kruzhilin. Vib. Spectrosc., 89 (2017) 75—80

30. N. N. Brandt, O. O. Brovko, A. Yu. Chikishev, O. D. Paraschuk. Appl. Spectrosc., 60 (2006) 288—293

31. H. J. Goren, M. Fridkin. Eur. J. Biochem., 41, N 2 (1974) 263—272

32. H. Gutfreund, J. M. Sturtevant. Biochem. J., 63, N 4 (1956) 656—661

33. K. K. Ghosh, S. K. Verma. Indian J. Biochem. Bio., 45, N 5 (2008) 350—353

34. P. A. Adams, E. R. Swart. Biochem. J., 161 (1977) 83—92

35. S. Verma. Indian J. Chem. A, 49 (2010) 1041—1046

36. M. L. Bender, G. R. Schonbaum, B. Zerner. J. Am. Chem. Soc., 84, N 13 (1962) 2562—2570

Review

For citations:

Balakhnina I.A., Brandt N.N., Mankova A.A., Chikishev A.Yu., Shpachenko I.G. DETERMINATION OF RATES OF α-CHYMOTRYPSIN-CATALYZED REACTIONS АT DIFFERENT TEMPERATURES AND pH BY RAMAN SPECTROSCOPY. Zhurnal Prikladnoii Spektroskopii. 2021;88(1):11-16. (In Russ.)

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ISSN 0514-7506 (Print)