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

Yiping Li; Wuba Yaq; Zaijie Jiang

doi:10.11158/saa.2.1.7

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Yiping Li,^1,2 Wuba Yaq,¹ Zaijie Jiang¹

¹Department of Biology, Beijing Normal University, Beijing 100875, China
²Institute of Zoology, Chinese Academy of Sciences, Beijing 100080, China

Abstract

Fresh eggs were collected daily from ovipositing female Haemaphysalis longicornis, homogenized and then centrifuged. The supernatant 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.

Citation Download Citation

Yiping Li, Wuba Yaq, and Zaijie Jiang "Purification and partial properties of vitellins from the tick Haemaphysalis longicornis (Acari: Ixodidae)," Systematic and Applied Acarology 2(1), 57-62, (1 July 1997). https://doi.org/10.11158/saa.2.1.7

Received: 17 November 1996; Published: 1 July 1997

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