Biopolym. Cell. 1988; 4(5):269-272.
http://dx.doi.org/10.7124/bc.000237
Short Communications
Endonuclease Mval dimerization induced by the oligonucleotide substrate
1Ovechkina L. G., 1Popova S. R., 1Zinoviev V. V., 2Vaitkevicius D. P., 2Janulaitis A. A., 1Gorbunov Yu. A., 1Malygin E. G.
  1. All-Union Research Institute of Molecular Biology
    Koltsovo, Novosibirsk Region, USSR
  2. Research and Production Amalgamation "Ferment"
    Vilnius, USSR

Abstract

Molecular weight of the endonuclease Mval was determined by the method of gel electrophoresis under denaturing conditions. The enzyme consists of a single polypeptide chain with molecular weight of 31300±400 dalton. Similar data are obtained by gel filtration and sucrose density gradient centrifugation. In the presence of substrate the oligonucleotide molecular weight of endonuclease Mval increases up to 53000±3000 dalton, that is related to protein dimerization during the formation of the enzyme-substrate complex.
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