Purification and partial characterization of vitellin from the eggs of the hard tick, Dermacentor variabilis


The major yolk proteins were purified from the eggs of the hard tick, Dermacentor variabilis using gel filtration and ion exchange chromatography. Two vitellin proteins were identified and designated vitellin A (480 kilodaltons; kDa) and vitellin B (370 kDa). The isolectric points were pH 6.1 and 6.25, respectively. The absorption maxima for both proteins were 280 and 400 nm. The buoyant density of vitellin A was 1.281 g/ml and vitellin B 1.278 g/ml. The vitellins were hemoglycolipoproteins as indicated by selective staining of polyacrylamide gels, carbohydrate analyses and lipid analyses. Under reducing conditions (SDS-PAGE), vitellin A had eight major polypeptides at 135, 110, 98, 80, 67, 50, 45, and 35 kDa. Vitellin B was identical to vitellin A with the addition of a 93 kDa subunit. The only carbohydrate detectable in the proteins was mannose. The neutral lipids detected in both proteins were cholesteryl esters, triglycerides, free fatty acids and their methyl esters, and cholestrol. The only detectable phospholipid in both proteins was phosphatidylethanolamine. The purified vitellins were immunologically identical to female hemolymph proteins but not to host hemoglobin. Antivitellin antibodies to vitellin were used to identify possible locations of vitellogenin in the organs of ovipositing females. © 1991.

Publication Title

Insect Biochemistry