Endonuclease Mval dimerization induced by the oligonucleotide substrate

Authors

  • L. G. Ovechkina All-Union Research Institute of Molecular Biology Koltsovo, Novosibirsk Region, USSR Author
  • S. R. Popova All-Union Research Institute of Molecular Biology Koltsovo, Novosibirsk Region, USSR Author
  • V. V. Zinoviev All-Union Research Institute of Molecular Biology Koltsovo, Novosibirsk Region, USSR Author
  • D. P. Vaitkevicius Research and Production Amalgamation "Ferment" Vilnius, USSR Author
  • A. A. Janulaitis Research and Production Amalgamation "Ferment" Vilnius, USSR Author
  • Yu. A. Gorbunov All-Union Research Institute of Molecular Biology Koltsovo, Novosibirsk Region, USSR Author
  • E. G. Malygin All-Union Research Institute of Molecular Biology Koltsovo, Novosibirsk Region, USSR Author

DOI:

https://doi.org/10.7124/bc.000237

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.

References

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Published

1988-09-20

Issue

Section

Short Communications