Subunit homologies of lactate dehydrogenase (LDH) isoenzymes between amphibians (Xenopus laevis) and mammals (Wistar rat) |
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| Affiliation: | 1. Department of Biomedical Sciences, Atlantic Veterinary College, University of Prince Edward Island, Charlottetown, PE, Canada;2. AVC Lobster Science Centre, Atlantic Veterinary College, University of Prince Edward Island, Charlottetown, PE, Canada;3. Department of Animal Science and Aquaculture, Faculty of Agriculture, Dalhousie University, Bible Hill, NS, Canada;4. EcoNov Inc., Moncton, NB, Canada;5. Homarus Inc., Shediac, NB, Canada;6. Canadian Rivers Institute, Department of Biology, University of Prince Edward Island, Charlottetown, PE, Canada |
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| Abstract: | - 1.1. The subunit distribution and subunit homologies of LDH isoenzymes were studied in the amphibian Xenopus laevis and in Wistar rats.
- 2.2. Several of the 11–15 isoenzymes of the pattern in Xenopus, separable by vertical starch gel electrophoresis, were purified, hybridized, and the cross-reaction of antibodies against the most positively charged isoenzyme with the isoenzymes present in tissue extracts of both species was tested.
- 3.3. The isoenzyme with the highest positive charge in Xenopus is a M-homotetramer homologous to mammalian LDH5.
- 4.4. The multibanded pattern of Xenopus LDH isoenzymes is very probably due to heterozygoty of the gene locus controlling the synthesis of M-subunits rather than to an epigenetic subbanding phenomenon.
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