Purification and partial properties of vitellins from the tick Haemaphysalis longicornis (Acari: Ixodidae)

Fresh eggs were collected daily from ovipositing female Haemaphysalis longicornis, homogenized and then centrifuged. The supematant was applied to a gel filtration column of Sepharose CL-4B and then to an ion exchange column of DEAE-cellulose (52); two vitellins (VnA and VnB) were purified. Native PAGE showed that VnA and VnB had equal molecular weights (about 220 kda). The female haemolymph at vitellogenesis period also showed Vn bands. Four similiar polypeptides (molecular weight about 67,64, 52,48 kda) for both VnA and VnB were demonstrated by SDS-PAGE.