Purification of elastase-like chymotrypsin from cardamom shoot and Capsule borer [corrected]
Artículo
en Inglés
| IMSEAR
| ID: sea-55901
ABSTRACT
An elastase-like chymotrypsin was purified by aprotinin-agarose affinity chromatography from the midgut extract of cardamom shoot and capsule borer, Conogethes punctiferalis. The purified enzyme had a Vmax of 687.6 +/- 22.1 nmole pNA released/min/mg protein, Km of 0.168 +/- 0.012 mM with SAAPLpNA as substrate and gave a single band on SDS-PAGE with a molecular mass of 72.1 kDa. Casein zymogram revealed one clear zone of proteolytic activity, which corresponded to the band obtained with SDS-PAGE indicating that this could be a single-polypeptide enzyme.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Conformación Proteica
/
Quimotripsina
/
Elastasa Pancreática
/
Inhibidores de Serina Proteinasa
/
Aprotinina
/
Cromatografía en Agarosa
/
Brotes de la Planta
/
Elettaria
/
Sistema Digestivo
/
Electroforesis en Gel de Poliacrilamida
Idioma:
Inglés
Año:
2007
Tipo del documento:
Artículo
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