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    Isolation and characterization of vitellin from the ovary of Penaeus monodon

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    Date
    1990
    Author
    Quinitio, Emilia T.
    Hara, Akihiko
    Yamauchi, Kohei
    Fuji, Akira
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    Abstract
    Female-specific protein (FSP, vitellogenin) in Penaeus monodon hemolymph and its related ovarian protein (vitellin, lipovitellin) were identified and characterized using electrophoretical and immunological procedures. The purification of vitellin from mature ovaries was carried out using hydroxylapatite and Sepharose 6B columns. Results indicated that there are two proteins specifically existing in the hemolymph of the mature female which are immunologically identical to ovarian protein. These are absent in the male. The isolated vitellin has a molecular weight of approximately 540 kDa and is composed of 4 major (polypeptide) subunits, 74, 83, 104 and 168 kDa and 1 minor (polypeptide) subunit, 90 kDa. The purified protein stained positively with periodic acid-Schiff and Sudan black B and thus is a glycolipoprotein.

    Results of double immunodiffusion demonstrate the cross-reactivity of P. monodon vitellin antiserum with the ovarian extract from mature females of Penaeus indicus, Penaeus merguiensis and Penaeus semisulcatus, but not with Pandalus kessleri, indicating that there is no antigenic difference at species level in Penaeidae.
    URI
    http://hdl.handle.net/10862/1225
    Suggested Citation
    Quinitio, E. T., Hara, A., Yamauchi, K., & Fuji, A. (1990). Isolation and characterization of vitellin from the ovary of Penaeus monodon. Invertebrate Reproduction and Development, 17(3), 221-227.
    DOI
    10.1080/07924259.1990.9672114
    Type
    Article
    ISSN
    0792-4259
    Subject
    Biochemical composition; Proteins; Penaeus monodon
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    • Journal Articles [1100]


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