1.
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.
Subject(s)
Animals , Aprotinin/pharmacology , Chromatography, Agarose , Chymotrypsin/isolation & purification , Digestive System/enzymology , Electrophoresis, Polyacrylamide Gel , Elettaria/parasitology , Fruit/parasitology , Larva , Lepidoptera/enzymology , Pancreatic Elastase/isolation & purification , Plant Shoots/parasitology , Protein Conformation , Serine Proteinase Inhibitors/pharmacology
2.
Indian J Biochem Biophys
;
1983 Jun; 20(3): 173-6
Article
in English
| IMSEAR
| ID: sea-26641
Subject(s)
Animals , Chymotrypsin/isolation & purification , Goats , Pancreas/enzymology , Sheep , Species Specificity
3.
Indian J Biochem Biophys
;
1976 Dec; 13(4): 335-8
Article
in English
| IMSEAR
| ID: sea-27165