Purification of elastase-like chymotrypsin from cardamom shoot and Capsule borer [corrected]
No Thumbnail Available
Date
2007-11-13
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
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.
Description
Keywords
Citation
Josephrajkumar A, Chakrabarty R, Thomas G. Purification of elastase-like chymotrypsin from cardamom shoot and Capsule borer [corrected] Indian Journal of Experimental Biology. 2007 Nov; 45(11): 998-1002