| Abstract: | The pattern of lactate dehydrogenase isozymes was investigated by means of electrophoresis in erythrocytes of CBA/Lac and DBA/2J mice homozygous for b and a alleles of the Ldr-1 locus. It is found that differences in the pattern of LDH isozymes, homozygous for the genes Ldr-1a and Ldr-1b, consist in increased activity of the isozyme LDH-4 in mice homozygous for the gene Ldr-1a (DBA/2J) within 12-14 days of postnatal development. Inhibition of the reaction between 125I-LDH-1 and the respective antibodies has demonstrated that increased LDH-4 activity during development is related to the higher content of B-subunits of LDH. It is suggested that the mechanism of the action of the gene Ldr-1 involves changes in the rate of the synthesis and degradation of B-subunit of LDH. |
