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- W2366868616 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 kDa, 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." @default.
- W2366868616 created "2016-06-24" @default.
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- W2366868616 date "2002-01-01" @default.
- W2366868616 modified "2023-09-24" @default.
- W2366868616 title "Purification, partial amino acid sequencing and identification of a cysteine proteinase in eggs of the cotton bollworm, Helicoverpa armigera" @default.
- W2366868616 hasPublicationYear "2002" @default.
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