Purification and Characterization of Arylphorin of the Chinese Oak Silkmoth, Antheraea pernyi

• Published in: International Journal of Industrial Entomology 2003, 6(1), , pp.33-44
• Main Authors: Park, Snag-Bong, Kim, Jeong-Wha, Kim, Soohyun, Park, Nam-Sook, Jin, Byung-Rae, Hwang, Jae-Sam, Seong, Su-Il, Lee, Bong-Hee, Park, Eunju
• Format: Article
• Language: Korean
• Subjects: Antheraea pernyi; Arylphorin; Chinese oak silkmoth; Lepidoptera; 농학
• ISSN: 1598-3579; 2586-4785

The arylphorin was purified from the pupal haemolymph of the Chinese oak silkmoth, Antheraea pernyi, and characterized physiologically and biochemically, The protein was purified by a simple preparative polyacrylamide gel electrophoresis (PAGE) and subsequent diffusive elution. The preparation was shown to be homogeneous by 7.5% native-PAGE. The native molecular weight of arylphorin was 450 kDa with a 80 kDa single subunit, suggesting hexamer, The protein contained high amounts (18.3%) of aromatic amino acids, phenylalanine (9.7%) and tyrosine (8.6%). Therefore, the protein was identified as a kind of a storage protein referred to as an arylphorin. The protein was stained by Schiff's reagent, suggesting a glycoprotein. The protein contained 4.9% (w/w) sugar and mannose and N-acetylglucosamine were major components. Also, degradation of the protein was begun by heat treatment at 90 for 20 minutes. These results showed that the A. pernyi arylphorin in the study is hexamer associated with the six subunits consisting of a 80kDa single subunit, and is different from that of Kajiura et al. (1998) in the subunit composition.