1. Purification of elastase-like chymotrypsin from cardamom shoot and Capsule borer [corrected].
- Author
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Josephrajkumar A, Chakrabarty R, and Thomas G
- Subjects
- Animals, Aprotinin pharmacology, Chromatography, Agarose, Digestive System enzymology, Electrophoresis, Polyacrylamide Gel, Fruit parasitology, Larva, Lepidoptera growth & development, Plant Shoots parasitology, Protein Conformation, Serine Proteinase Inhibitors pharmacology, Chymotrypsin isolation & purification, Elettaria parasitology, Lepidoptera enzymology, Pancreatic Elastase isolation & purification
- 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. more...
- Published
- 2007