Vitellogenin (Vg), the yolk precursor protein and its product vitellin (Vn) have been identified in hemolymph and fat body of females and mature oocytes in the millipede Spirostreptus asthenes employing double immunodiffusion technique. These two proteins are absent in males indicating that they are female specific. Immunoelectrophoresis has shown that there is only one vitellogenic protein present in S. asthenes. Vg and Vn were isolated by gel filtration. Polyacrylamide gel electrophoresis (PAGE) analysis revealed that Vg and Vn are glycolipoproteins. Vg contains 48.8% protein, 2.2% carbohydrate and 48.9% lipid. Vn is comprised of 52% protein, 2.3% carbohydrate and 45.4% lipid. The lipid components of Vg and Vn include mainly phospholipids such as phosphatidic acid, sphingomyelin, phosphatidyl choline, phosphatidyl ethanolamine and cholesterol. On SDS-PAGE analysis both Vg and Vn yielded five sub units each. The molecular weight of the sub units of Vg was found to be 135, 115, 105, 73 and 56 kDa and those of Vn were 125, 110, 100, 68, and 53 kDa. The vitellogenic system of S. asthenes resembles that of insects. The phylogenetic relationship of the vitellogenic system of this millipede with other arthropod groups is discussed. © 1991.
Prasath, E. B., & Subramoniam, T. (1991). Vitellogenin and vitellin of a millipede Spirostreptus asthenes: Occurrence, isolation and partial characterization. Insect Biochemistry, 21(8), 865–870. https://doi.org/10.1016/0020-1790(91)90093-T