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An ontogenetic study of lactate dehydrogenase in Porocephalus crotali (Pentastomida)

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, ISSN: 0305-0491, Vol: 53, Issue: 3, Page: 325-328
1976
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1.1. The ontogenetic study of lactate dehydrogenase from Porocephalus crotali was undertaken using specific activities, optimal pH values, isoelectric points, Michaelis-Menten constants for lactate and nicotinamide adenine dinucleotide (NAD) and polyacrylamide-gel electrophoresis.2.2. Large changes in specific activities were noted, ranging from 3·6 in the infective egg to 13·5 in the infective nymph and 12·8 in the adult.3.3. Optimal pH ranged from 7·9 to 8·1 and small changes in Km's for lactate and NAD in all three developmental stages were observed.4.4. Anodal polyacrylamide-gel electrophoresis of Porocephalus crotali eggs, larvae, and adults has shown lactate dehydrogenase to consist of one, five, and five isoenzymes, respectively.5.5. LDH-4 is the predominant fraction in the nymphal and adult stages.6.6. In terms of electrophoretic mobility, LDH-1 of eggs corresponds to LDH-1 in the nymph and adult stages.7.7. Dramatic differences were found when the protein and lipoprotein patterns of the eggs, nymphs and adults were compared.8.8. These differences were in the electrophoretic mobility, number and density of the protein and lipoprotein fractions.9.9. Isoelectric focusing demonstrated five molecular forms of LDH from the nymph and adult stages while only one was found for the egg.

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