Purification, characterization, and synthesis of vitellin from the cabbage butterfly Pieris rapae L.

Hak R. Kim, Young-Gyu Ko, Richard T. Mayer

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    10 Citations (Scopus)


    Vitellin from the cabbage butterfly Pieris rapae L. was purified and characterized by electrophoresis. Vitellin from P. rapae is a phosphorylated glycolipoprotein of 380,000 ± 10,000 molecular weight as determined by nondenaturing polyacrylamide gel electrophoresis. Two subunits with an Mr of 150,000 and 40,000 were obtained from vitellin. The native molecule is thought to be a tetramer composed of two molecules of each of these subunits. The isoelectric point, as determined by isoelectric focusing on polyacrylamide gels, is 6.10. Vitellin and vitellogenin were indistinguishable by immunological methods such as double diffusion and tandem‐crossed immunoelectrophoresis. Vitellogenin from the hemolymph and vitellin from the ovary were quantified by rocket immunoelectrophoresis. Vitellogenin and vitellin were first detected in 6‐day‐old pupae, and their levels increased continuously during ovarian development. Vitellogenin synthesis by the fat body in 4‐day‐old female pupae could be induced by juvenile hormone I.

    Original languageEnglish
    Pages (from-to)67-79
    Number of pages13
    JournalArchives of Insect Biochemistry and Physiology
    Issue number1
    Publication statusPublished - 1988


    • immunoelectrophoresis
    • juvenile hormone
    • vitellogenin

    ASJC Scopus subject areas

    • Physiology
    • Biochemistry
    • Insect Science


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