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Biol Bull 132: 299-310. (June 1967)
© 1967 Marine Biological Laboratory
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AMYLASE AND GLYCOGENOLYSIS IN AMPHIBIAN DEVELOPMENT

FRANCISCO D. BARBIERI 1, JORGE S. RAISMAN 1, and CÉSAR ALBARRACIN 1

1 Instituto de Biología and Instituto de Química Biológica, Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán, R. Argentina

1. An enzyme with the properties of a mammalian agr-amylase in the eggs of the toad Bufo arenarum is described. The enzyme appears associated in a very labile fashion to particles sedimenting at 1500 g for 20 minutes in 0.25 M sucrose solution.

2. Egg glycogen is polydisperse and does not seem to be linked to the same particles to which amylase appears associated. At the beginning of development it reacts with iodine in a different way than liver glycogen of the same species, as was shown by their absorption spectra; after gastrulation, when glycogen is supposed to be actively metabolized, the spectra of embryo and adult glycogens become similar.

3. Some evidence is presented indicating that egg glycogen in the course of development is degraded by the action of amylase, which would be progressively released from its compartment.






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Copyright © 1967 by the Marine Biological Laboratory.