Biopolym. Cell. 1987; 3(3):152-154.
http://dx.doi.org/10.7124/bc.0001E7
Short Communications
Dimerization of EcoDam-methylase induced by the oligonucleotide substrate
1Rechkunova N. I., 1Zinoviev V. V., 1Malygin E. G., 2Gorbunov Yu. A., 2Popov S. G., 1Nesterenko V. F., 2Buriyanov Ya. I.
  1. All-Union Research Institute of Molecular Biology
    Koltsovo, Novosibirsk Region, USSR
  2. Institute of Biochemistry and Physiology of Microorganisms, Academy of Sciences of the USSR
    Pushchino, Moscow Region, USSR

Abstract

The Ecodam-methylase has been investigated for its interaction with the 20-base oligonucleotide duplex containing the enzyme recognition site. An increase of the enzyme molecular weight was detected by the gel-filtration and sucrose density gradient centrifugation methods. The maximal value of the molecular complex weight was observed when concentrations of the enzyme and the substrate were equal. The results obtained prove the formation of the dimeric enzyme form in the substrate presence.
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References

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