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Yolk proteins in developing follicles of the house cricket,Acheta domesticus (L.)

✍ Scribed by Nicolaro, Mary-Lou ;Bradley, James T.


Book ID
102891481
Publisher
John Wiley and Sons
Year
1980
Tongue
English
Weight
592 KB
Volume
212
Category
Article
ISSN
0022-104X

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✦ Synopsis


Abstract

The occurence of the two major yolk proteins in vitellogenic follicles at various stages of development in the house cricket, Acheta domesticus, was studied electrophoretically. Follicles were staged into size classes ranging from 0.75 mm (stage I) to β‰₯2.0 mm (stage IV) for unfertilized eggs (chorionated follicles) and the molar ratio of the two vitellins within follicles of each stage determined. The ratio of vitellin I to vitellin II during the early stages of vitellogenesis was found to be greater than that during later stages, suggesting the possibility of changing selectivity of vitellogenin uptake by follicles as they progress through the vitellogenic phases of oogensis. The relative distribution of vitellins I and II within the cytoplasm of unfertilized, chorionated follicles was studied by sectioning stage IV follicles into thirds and determining the molar ration of vitellin I to II in each third. It was found that a differential distribution of each vitellin is established during oogenesis such that vitellin I is present in greater quantities in the posterior region and vitellin II in greater quantities in the anterior region of the follicle.

The molecular weights of the two vitellins were estimated using native polyacrylamide gels of varying percents acrylamide. The molecular weights of vitellins I and II were estimated at 352,000 and 327,000 daltons, respectively.


πŸ“œ SIMILAR VOLUMES


Yolk proteins in the house cricket,Achet
✍ Bradley, James T. ;Edwards, John S. πŸ“‚ Article πŸ“… 1978 πŸ› John Wiley and Sons 🌐 English βš– 749 KB

## Abstract Four female‐specific yolk proteins were identified in the hemolymph of adult, ovulating __Acheta domesticus__ through the use of SDS‐polyacrylamide gel electrophoresis. Molecular weights were estimated at 130,000; 97,000; 49,000; and 47,000 daltons, and all four proteins stained PAS‐pos