Purification and Partial Characteriza6tion of the Storage Protein-like Protein from the 5th Instar Latval Haemolymph of the Chinese Oak Silkworm, Antheraea pernyi.

  • Park, Nam-Suk (Miyang National University, Miryang, Kyong Nam) ;
  • Lee, Sang-Mong (Miyang National University, Miryang, Kyong Nam) ;
  • Moon, Jae-Yu (College of Agriculture and Life Secience, Seoul National University, Suwon) ;
  • Su, Il-Seong (The University of Suwon)
  • Published : 1999.09.01

Abstract

The storage protein-like protein has been purified from the 5th instar larval haemolymph of the Chinese osk silkwom, Antheraea pernyi, and the preparation was shown to be homogeneous by 7.5% native-PAGE. The molecule was consisted of a single subunit with a molecular weight of 80K, but the number of the subunits was not determined. The protein was defied as glycoprotein by Schiff's regent stining. Rabbit antibody prepared against the purified protein crotein crossreacted with the 5th instar larval haemolymph proteins of Antheraea pernyi and antheraea yamamai, but not with those of Bombyx mori and Bombyx mandarina.

Keywords

References

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