A novel electrophoretic technique designed to modify the ratio of magnesium isotopes inside the creatine kinase active sites. A preliminary report

Isotopes in Environmental and Health Studies

Volumn 40, Issue 3, 2004, Pages 221-227

  Kouznetsov, Dmitri A ^a   Arkhangelsky, Stanislav E ^a   Berdieva, Alana G ^b   Khasigov, Peter Z ^b   Orlova, Marina A ^c  

^a SEMENOV INSTITUTE OF CHEMICAL PHYSICS   (Russian Federation)

^b I M SECHENOV FIRST MOSCOW STATE MEDICAL UNIVERSITY   (Russian Federation)

^c MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Creatine kinase; Isotope effect; Isotope enrichment; Magnesium 25; Spin selective process

Indexed keywords

CREATINE KINASE; ISOTOPE; MAGNESIUM;

ELECTROCHEMISTRY;

ARTICLE; BINDING SITE; ELECTROPHORESIS; METABOLISM; METHODOLOGY;

BINDING SITES; CREATINE KINASE; ELECTROPHORESIS; ISOTOPES; MAGNESIUM;

EID: 4544232302     PISSN: 10256016     EISSN: None     Source Type: Journal    
DOI: 10.1080/10256010410001689916     Document Type: Article

References (23)

1. Wyss, M., Smeiting, J., Wevers, R. A. and Wallimann, T. (1992). Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism. Biochim. Biophys. Acta 1102, 119-166.
2. Webb, T. I. and Morris, G. E. (2001). Structure of an intermediate in the unfolding of creatine kinase. Proteins 42, 269-278.
3. 3-creatine transition state analogue complex. Biochemistry 41, 13861-13867.
4. Kouznetsov, D. A., Khasigov, P. Z. and Orlova, M. A. (2003). Creatine kinase, an ATP-generating enzyme, in the venom of Viperiae. Biomed. Chem. 49, 289-296.
5. Grossman, S. H., France, R. M. and Matheis, J. R. (1992). Heterogenous flexibilities of the active-site domains of homodimeric creatine kinase: Effect of substrate. Biochem. Biophys. Acta 1159, 29-36.
6. Fritz-Wolf, K., Schneider, T., Walliman, T. and Kabsch, W. (1996). Structure of mitochondrial creatine kinase. Nature 381, 341-345.
7. Raimbault, C., Buchet, R. and Vial, C. (1996). Changes in creatine kinase secondary structure induced by the release of nucleotides from caged compounds. An infrared difference-spectroscopy study. Eur. J. Biochem. 240, 134-142.
8. Kenyon, G. L. (1996). Energy metabolism. Cteatine kinase shapes up. Nature 381 (6580), 281-282.
9. Buchachenko, A. L. (1993). Magnetic isotope effect in the chemical reactions mechanism. Russ. Chem. Rev. 62, 1073-1082.
10. Buchachenko, A. L. (2001). Magnetic isotope effect: nuclear spin control of chemical reactions. J. Phys. Chem. A105, 9995-10011.
11. Grissom, C. B. (1995). Magnetic field effects in biology: a survey of possible mechanisms with emphasis on radical-pair recombination. Chem. Rev. 95, 3-24.
12. Akoyev, I. G., Pashovkina, M. S., Dolgacheva, L. P., Semenova, T. P. and Kalmykov, V. L. (2002). Enzymatic activity and a possible role of microwave effects in free radical biomedical research. Radiat. Biol. Radioecol. 42, 322-330.
13. Laemmli, U. L. (1970). An efficient gradient polyacrylamide gel electrophoresis system for protein separation. Nature 227, 690-685.
14. Kouznetsov, D. A., Govorkov, A. V., Zavijalov, N. V., Sibileva, T. M., Richter, V. and Drawczek, J. A. (1986). Fast estimation of ATP/ADP ratio as a special step in pharmacological and toxicological studies using the cell-free translation system. J. Biochem. Biophys. Methods 13, 53-56.
15. Kouznetsov, D. A., Zavijalov, N. V., Govorkov, A. V. and Ivanov, A. A. (1986). Methyl mercury induced combined inhibition of ATP regeneration and protein synthesis in reticulocyte lysate cell-free translation system. Toxicol. Letters 30, 267-271.
16. Bradford, M. M. (1976). An improved colorimetric technique for protein measurement. Analyt. Biochem. 72, 348-354.
17. Devenyi, T. and Gergely, J. Amino acids, peptides and proteins: biochemical and immunological techniques in protein chemistry. Elsevier Scientific Publ.: Amsterdam, London, New York, 1974, pp. 88-94.
18. Bouchet, J. S. and Telashima, O. Metal ions detection in biomedical studies. Fundamentals and applications. Alba Regia: Szeged-Budapest, 1999, pp. 116-130.
19. Bommarius, A. S. and Riebel, B. Biocatalysis. Wiley Publ.: Atlanta, New York, Toronto, London, 2002, pp. 100-110.
20. Scopes, R. K. Protein purification. Springer-Verlag: New York, 1987, pp. 167-189.
21. Ivanov, A. A. Recent criticisms on the radiocarbon method accuracy in the light of biofractionation of C-isotopes and related molecular phenomena studies. In: Advances in Archaeological Biomaterials Research (Ed. T. Baglioni). University Press: Turin, 2000, pp. 70-92.
22. 3HgCl. J. Phys. Chem. 108A, 707-710.
23. Buchachenko, A. L. and Kouznetsov, D. A. (2003). Methylmercury chloride in thiol kinases inhibition studies: Hg isotopy effect. Arch. Exptl. Biol. Med. 49, 611-617.