Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/5359
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dc.contributor.authorJosephrajkumar, A-
dc.contributor.authorChakrabarty, R-
dc.contributor.authorThomas, G-
dc.date.accessioned2009-07-20T10:10:56Z-
dc.date.available2009-07-20T10:10:56Z-
dc.date.issued2007-11-
dc.identifier.issn0975-1009 (Online); 0019-5189 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/5359-
dc.description998-1002en_US
dc.description.abstractAn 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.en_US
dc.language.isoen_USen_US
dc.publisherCSIRen_US
dc.sourceIJEB Vol.45(11) [November 2007]en_US
dc.subjectAprotininen_US
dc.subjectCardamomen_US
dc.subjectChymotrypsinen_US
dc.subjectConogethes punctiferalisen_US
dc.subjectTrypsinen_US
dc.titlePurification of elastase-like chymotrypsin from cardamom shoot and Capsule boreren_US
dc.typeArticleen_US
Appears in Collections:IJEB Vol.45(11) [November 2007]

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