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|Title:||Purification of elastase-like chymotrypsin from cardamom shoot and Capsule borer|
<i style="">Conogethes punctiferalis</i>
|Abstract:||An elastase-like chymotrypsin was purified by aprotinin-agarose affinity chromatography from the midgut extract of cardamom shoot and capsule borer, <i style="">Conogethes punctiferalis</i>. The purified enzyme had a V<sub>max </sub>of 687.6 ± 22.1 nmole <i style="">p</i>NA released/min/mg protein, K<sub>m</sub> of 0.168 ± 0.012 m<i style="">M</i> with SAAPL<i style="">p</i>NA 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.|
|ISSN:||0975-1009 (Online); 0019-5189 (Print)|
|Appears in Collections:||IJEB Vol.45(11) [November 2007]|
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