›› 2002, Vol. 45 ›› Issue (6): 840-843.

• RESEARCH PAPERS • Previous Articles     Next Articles

Purification, partial amino acid sequencing and identification of a cysteine proteinase in eggs of the cotton bollworm, Helicoverpa armigera

ZHANG Zhi-Hong, ZHAO Xiao-Fan*, WANG Jin-Xing   

  • Online:2002-12-20 Published:2002-12-20

Abstract: A cysteine proteinase from cotton bollworm eggs was purified by anion-exchange chromatography based on previous work. The proteinase gave a single band after SDS-PAGE. The molecular mass of the purified proteinase was estimated to be 29 kD, which showed proteolytic activity in an in situ hydrolysis experiment. A partial amino acid sequence was compared with that of other typical proteinases. Similarities were appreciable between the composition of the egg proteinase and cysteine proteinases, particularly cathepsin B.

Key words: Helicoverpa armigera, cysteinase proteinase, purification, amino acid sequence, identification