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U.S. Department of Energy
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Vitellogenin of the tobacco hornworm, Manduca sexta: properties and endocytotic incorporation into follicles

Thesis/Dissertation ·
OSTI ID:6701214
Manduca sexta vitellogenin is a phosphoglycolipoprotein (M/sub r/ approx. 500,000) that contains two copies of the apoproteins 13% lipids, 3% carbohydrates and 0.6% phosphorus. The two apoproteins are immunologically distinct and apovitellogenin-II is not completely accessible to the aqueous environment in the intact molecule. The carbohydrate moiety located on apovitellogenin-I has a high mannose structure. Follicle membranes bind /sup 125/I-labeled vitellogenin with high affinity and specificity. Total binding sites were estimated at 4 x 10/sup 14/ sites/g of follicle membrane protein. The binding was sensitive to pH and calcium. Competition studies showed that binding of vitellogenin was blocked by vitellin and deglycosylated vitellogenin but not by lipophorin, microvitellogenin or apovitellogenin-II. These results suggest that the uptake of vitellogenin involves binding to specific receptors on follicle membranes and the carbohydrate moiety and apovitellogenin-II are not involved in the interaction with the receptors.
Research Organization:
Arizona Univ., Tucson (USA)
OSTI ID:
6701214
Country of Publication:
United States
Language:
English