Biopolym. Cell. 1989; 5(6):39-46.
http://dx.doi.org/10.7124/bc.0000F5
Structure and Function of Biopolymers
Homologous character of amino acid sequences of superoxide dismutases and proteins coded for by mitochondrial genome
1Beregovskaya N. N., 1Savich A. V.
  1. Institute of Surface Chemistry, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR
  2. Institute of Biophysics, Ministry of Public Health of the USSR
    Moscow, USSR

Abstract

The degrees of homologous character between amino acid sequences of 4 types of superoxide dismutases (Cu/Zn-SOD, Fe-SOD, Mn-SOD bacterial, Mn-SOD mitochondrial) and fragments of the carboxyl ends of NADH dehydTogenases coded for by rnitochondrial genome (iND4) were estimated. The alignement of lamino acid sequences of SOD and NADH-dehydTOgenase was performed in opposite directions. The highest degree of homology was found between ND4 and mitoclhondrial Mn-!SiOD. Degrees of homology between amino acid and nucJeotide sequences for subunits of ND complexe coded for by mitochondrial genome and bacterial ND were calculated. The evolutionary scheme including mitochondrial and bacterial ;ND- and bacterial Mn-SOD is given.
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