Journal of Biosciences

, Volume 20, Issue 2, pp 211–223 | Cite as

Developmental regulation of silk protein P25 in the silkwormBombyx mori

  • K Muthumani
  • S Mathavan
  • S Mayilvahanan


P25 protein was extracted from cocoons of the silkwormBombyx mori by alkali solubilization and purified by gel elution. The purity and authenticity of the protein were confirmed by SDS-PAGE, 2-dimensional gel electrophoresis and peptide mapping. Polyclonal anti-P25 sera were raised in rabbit and mice. The relative abundance of P25 protein present in the larva during different developmental stages was analysed by SDS-PAGE, and quantified by sandwich ELISA. The minimum level (0.2 μg/animal) of this protein was recorded at the beginning of the first instar and maximum (16.7mg/pair of silkgland) on the final day of the V instar. During each moult period, P25 protein level was suppressed; the level increased with the initiation of feeding and reached maximum on the 3rd day of each instar except the final instar where the maximum was recorded prior to pupal moult. Western blot analysis also confirmed the developmental stage-specific accumulation of P25 protein in the silkwormBombyx mori.


Bombyx mori P25 protein purification and quantification stage-specific regulation 


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Copyright information

© Indian Academy of Sciences 1995

Authors and Affiliations

  • K Muthumani
    • 1
  • S Mathavan
    • 1
  • S Mayilvahanan
    • 1
  1. 1.Sericulture Research Unit, Department of Genetics, School of Biological SciencesMadurai Kamaraj UniversityMaduraiIndia

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