No preferential activation of the maternally derived alcohol dehydrogenase (ADH) allele was found in any of the chicken male x Japanese quail female hybrids examined. ADH activity in the liver was, in fact, found to exist in two different cathodal zonal regions on starch gel electropherograms; the z
Ontogeny of lactate dehydrogenase isozymes in chicken-quail hybrid embryos
β Scribed by Peter G. Meyerhof; Leslie E. Haley
- Publisher
- Springer
- Year
- 1975
- Tongue
- English
- Weight
- 695 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0006-2928
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β¦ Synopsis
The ontogeny of lactate dehydrogenase (LDH) isozymes was examined in avian hybrids and compared with the isozyme patterns of the parental species. Hybrids were obtained by crossing female Japanese quail (Coturnix coturnix japonica) with male domestic chickens (Gallus gallus domesticus). By use of starch gel electrophoresis and an enzyme-specific stain, traces of embryonic paternally derived L D H were detected in unineubated hybrid eggs. B was concluded that the embryonic genes eoding for the B subunits of L D H are activated during the hours between fertilization and oviposition. In early blastoderms, a great excess of maternally stored L D H is present. In the hybrid, the predominantly maternal pattern of isozymes shifts during embryogenesis to a predominantly paternal pattern. This was considered evidence for differential allelie regulation of L D H inactivation. A progressive trend toward the establishment of the adult distribution of isozymes in various tissues was also observed in the hybrid and quail, and found to be similar to chicken LDH isozyme ontogeny.
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