Lactic dehydrogenase isozyme patterns and alpha-hydroxybutyrate dehydrogenase activities in serum from newborns, patients with ovarian cancer or myocardial infarction

Lactic dehydrogenase (LDH) and alpha-hydroxybutyrate dehydrogenase (HBD) and LDH isozyme patterns were studied in serum from newborns and patients with ovarian cancer or myocardial infarction. LDH and HBD activities from newborns and patients with ovarian cancer or myocardial infarction were significantly increased, compared with those from patients with benign ovarian tumor. These increases were accompanied with a decrease of LDH-H and an increase of LDH-M in serum from newborns and patients with ovarian cancer, while an increase of LDH-H in serum from patients with myocardial infarction was dominant. However, the raised HBD activities in serum from patients with benign ovarian tumor did not affect the LDH isozyme patterns. From analysis of linear regression, a negative correlation between LDH-1 or -2 and HBD activity in serum from patients with ovarian cancer was observed while there was a positive correlation between LDH-4 and HBD activity. Similar patterns in serum from newborns were observed. On the other hand, a positive correlation between LDH-1 and HBD activity and a negative correlation between LDH-4 and HBD activity were found in serum from patients with myocardial infarction.     

Probable evolutionary mechanism underlying octanol dehydrogenase isozyme patterns in the genus drosophila

Summary A comparative species study of octanol dehydrogenase (ODH) isozyme patterns of members of the genusDrosophila and six related genera has shown a rough correlation of these with taxonomic grouping at the level of subgenus or section within the subgeneraPholadoris, Sophophora, andDrosophila. Extensive polymorphism of ODH patterns occurs in thequinaria section of the subgenusDrosophila. In polymorphic strains ofD. pellewae andD. metzii, ODH pattern types of single females were shown to occur in frequencies expected on the hypothesis of a Hardy-Weinberg distribution of morphs depending on alleles at a single locus. However, patterns of homozygous B and A variants extracted from such populations differ from those expected if variants are due to alleles at a structural locus and indicate that such variants differ in alleles affecting the levels of particular isozymes. ODH patterns of monomorphic species strikingly resemble those of homozygous B, D, or A variants extracted from polymorphic populations ofD. pellewae, D. metzii, orD. albirostris which have been studied genetically by Pipkin (1968a, 1969) and Ogonji (1971). Based on these findings and previous work indicating that the ODH molecule is a polymer, an hypothesis is proposed that species differences in ODH patterns depend on differential activity of several ODH structural genes.This work was supported by NIH grant GM 18409-01 and NSF grant GB 8779.     

Changes in the activity and isozyme patterns of malate dehydrogenase in root nodules of yellow lupine

The malate dehydrogenase present in the cytoplasmic fraction of plant origin and bacteroids from yellow lupine root nodules was investigated. The plant enzyme was 14 times more active in nodules than in roots and it contained 6 molecular forms in nodules compared with 3 forms detected in roots. The highest malate dehydrogenase activity in plant fraction and bacteroids was noted in 50-day old plants. Changes in the isoenzymatic patterns of malate dehydrogenase in plant fraction and bacteroids accompanying ageing of the lupine root nodules were observed. Possible physiological role of malate pathway in metabolism of lupine root nodules is discussed.     

Lactate dehydrogenase isozyme patterns in the denervated quail (Coturnix coturnix japonica) muscles

Polyacrylamide gel electrophoresis of the Japanese quail (Coturnix cotunix japonica) muscle extracts revealed a single lactate dehydrogenase isozyme. A month after surgical unilateral brachiotectomy (denervation) there was significant atrophy of the triceps, biceps and radius ulnar muscles accompanied by the appearance of an additional lactate dehydrogenase isozyme band. This extra band may be the result of the synthesis of a new lactate dehydrogenase isozyme. This new isozyme exhibited a lower affinity for lactate, less sensitivity to urea denaturation and was more thermostable than the lactate dehydrogenase of normal (innervated) quail muscles. Based on these properties, it is suggested that the newly synthesised isozyme of the denervated muscles is LDH-1, (or B4/H4) type. Brachiotectomy also resulted in significant quantitative changes in the total lactate dehydrogenase activity of innervated muscles of the same animal.