Purification of elastase-like chymotrypsin from cardamom shoot and Capsule borer [corrected].
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.
Josephrajkumar
A
A
Cardamom Research Station, Kerala Agricultural University, Pampadumpara 685 556, Dist. Idukki, India. entojoe2003@yahoo.co.in
Chakrabarty
R
R
Thomas
G
G
D000818:Animals; D007611:Aprotinin / Q000494:pharmacology; D002847:Chromatography, Agarose; D002918:Chymotrypsin / Q000302:isolation & purification*; D004064:Digestive System / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D028523:Elettaria / Q000469:parasitology*; D005638:Fruit / Q000469:parasitology; D007814:Larva; D007915:Lepidoptera / Q000201:enzymology* / Q000254:growth & development; D010196:Pancreatic Elastase / Q000302:isolation & purification*; D018520:Plant Shoots / Q000469:parasitology; D011487:Protein Conformation; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology
D015842:Serine Proteinase Inhibitors; D007611:Aprotinin; D002918:Chymotrypsin; D010196:Pancreatic Elastase