Acclimation of Misgurnus fossilis to 5 and 18 degrees C induced considerable changes in LDH-A gene expression in white skeletal muscle. Qualities of total and messenger RNA isolated from weighted portions of muscle are considerably higher after acclimation to 18 degrees C as compared to 5 degrees C. However, a PCR assay of cDNA synthesized from these mRNA and equalized by optical density demonstrated that the level of LDH-A gene expression was indistinguishable for high and low acclimation temperatures, while expression of other genes (glyceraldehyde-3-phosphate dehydrogenase and alpha-actin) considerably increased at 18 degrees C as compared to 5 degrees C. The specific enzymatic activity of LDH from white skeletal muscle of the fish acclimated to low temperature is by 20% higher than that for high-temperature acclimation. Structural analysis of the PCR products synthesized on cDNA-5 degrees C and cDNA-18 degrees C has revealed no differences. However, there are indirect indications of the differences in the C-thermal region of the LDH-A molecule. Northern hybridization reveals the differences at the RNA level: one (1400 bp) or two (about 1600 and 1400 bp) hybridization signals have been found in mRNA-5 degrees C and mRNA-18 degrees C, respectively. The presence of two fractions in the mRNA-18 degrees C indicates alternative splicing.