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
Dmitri A KouznetsovMarina A Orlova

Abstract

A simple and efficient preparative electrophoretic technique has been proposed to obtain a modified creatine kinase (CK, E.C.2.7.3.2) molecule with an increased content of 25Mg in the active site. A key point of the method is the special design of a 0.9 x 12.0 cm column for ascendent electrophoresis, packed consecutively, from the bottom to the top, with layers of 30 % PAAG (polyacrylamide grade), 25Mg2+ -containing 7.5 % PAAG, enzyme-binding ADP Sepharose and 2.2 % agarose gels, based on different tris-glycine and tris-HCl separation buffer systems. The isotope substitution process was a result of simultaneous desorption of enzyme from ADP Sepharose and electrically directed extensive flow of 25Mg2+ cations through the porous gel matrix. Greater than 8-fold 25Mg enrichment, i.e. a 10.2-86.3 % increase of 25Mg contribution to total enzyme magnesium, has been reached. The modified 25Mg-rich CK samples manifest higher (2.4-fold increase) values of specific catalytic activity when compared with intact (control) ones.

References

Sep 25, 1992·Biochimica Et Biophysica Acta·M WyssT Wallimann
May 23, 1996·Nature·G L Kenyon
May 23, 1996·Nature·K Fritz-WolfW Kabsch

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Citations

Dec 27, 2011·Proceedings of the National Academy of Sciences of the United States of America·Darragh CrottyJ M D Coey
Jan 27, 2012·Chemical Reviews·Anatoly L BuchachenkoNatalia N Breslavskaya
Feb 6, 2008·The Journal of Physical Chemistry. B·Anatoly L BuchachenkoMarina A Orlova

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