Purification of elastase-like chymotrypsin from cardamom shoot and Capsule borer [corrected]
Article
in English
| 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.
Full text:
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Index:
IMSEAR (South-East Asia)
Main subject:
Protein Conformation
/
Chymotrypsin
/
Pancreatic Elastase
/
Serine Proteinase Inhibitors
/
Aprotinin
/
Chromatography, Agarose
/
Plant Shoots
/
Elettaria
/
Digestive System
/
Electrophoresis, Polyacrylamide Gel
Language:
English
Year:
2007
Type:
Article
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