Biopolymers and cell. 1988. Volume 4. № 5. 269 - 272

L. G. Ovechkina, S. R. Popova, V. V. Zinoviev. D. P. Vaitkevicius A. A. Janulaitis , Yu. A. Gorbunov, E. G. Malygin

ENDONUCLEASE Mval DIMERIZATION INDUCED BY THE OLIGONUCLEOTIDE SUBSTRATE

Summary

    Molecular weight of the endonuclease Mval was determined by the method of gel electro-phoresis 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 oligo-nucleotide 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.