| Literature DB >> 28305116 |
Sachiko Takesue1, Kazuo Onitake1, Hiroomi Keino2, Yoshiki Takesue3.
Abstract
Vitellin was purified from eggs of the silkworm,Bombyx mori, by a new method in which vitellin was extracted from isolated yolk granules. The purified vitellin had a molecular weight of 540,000. An antibody against purified vitellin was prepared in rabbits. It reacted with the hemolymph vitellogenin as well as with purified vitellin, but not with other proteins in the hemolymph or in the extract from yolk granules. The anti-vitellin IgG was used to immunocytochemically locate vitellin in theBombyx non-diapause egg during early developmental stages. In the egg, just after oviposition, vitellin was located in internal yolk granules and in small yolk granules of the periplasm. During the early developmental stages studied, vitellin was not metabolized uniformly throughout the egg. The vitellin of the internal yolk granules located at the posterior-dorsal part and of the small peripheral yolk granules was utilized in 16 h and 2 days, respectively, after oviposition. A thin, very vitellin-poor layer was located between the periplasm and the vitellin-rich interior in the newly laid egg. it was always in close contact with the periphery where blastoderm and germ-band cells developed.Entities:
Keywords: Embryogenesis; Immunocytochemistry; Silkworm; Vitellin; Yolk granule; Yolk protein
Year: 1983 PMID: 28305116 DOI: 10.1007/BF00848679
Source DB: PubMed Journal: Wilehm Roux Arch Dev Biol ISSN: 0340-0794