• The Korean Journal of Zoology
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• v.35 no.1
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• pp.17-22
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• 1992

The three yolk polypeptides have been isolated and partially characterized. Their molecular weights of YPI, YP2, and YP3 were 48, 000, 47, 000, and 46, 000, respectivelv, as judged by SDS-polyacrvlamide gel electrophoresis. They have different digestion products upon in situ peptide mapping by limited proteolysis. Two-dimensional gel electrophoresis showed that their isoelectric points were heterogeneous from 5.92 to 6.54. And thew showed three different antigen-antibody reactions when each polvpeptides is reacted with antisera made to a mixture of all of three. These data reported here indicate that the yolk proteins are consisted of distinctive polypeptides in Drosophlla sp. (robusta species group).