Developmental regulation of silk protein P25 in the silkworm Bombyx mori.
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Date
1995-03
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Abstract
P25 protein was extracted from cocoons of the silkworm Bombyx 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 silkworm Bombyx mori.
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Keywords
Bombyx mori, P25 protein purification and quantification, stage-specific regulation
Citation
Muthumani K, Mathavan S, Mayilvahanan S. Developmental regulation of silk protein P25 in the silkworm Bombyx mori. Journal of Biosciences. 1995 Mar; 20(2): 211-223.