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dc.contributor.authorJanarthanan, S-
dc.contributor.authorVenugopal, K J-
dc.contributor.authorIgnacimuthu, S-
dc.identifier.issn0975-1009 (Online); 0019-5189 (Print)-
dc.description.abstractα-amylase inhibitor, a seed storage protein, is quantified in different wild pulses. These wild pulses when tested for their relative resistance to the bruchid, C. maculatus, showed that most of the developmental parameters of the pest are significantly affected. The wild variety of the species, Lablab purpureus with brown seed coat which contains a higher amount of the inhibitor was selected for purification and characterisation. α-amylase inhibitor purified from this variety has a molecular weight of 65 kDa in non-denaturing electrophoretic gel which resolved into three polypeptides of 14, 17 and 20 kDas respectively in denaturing electrof1horetic gel.en_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJEB Vol.37(08) [August 1999]en_US
dc.titlePurification and characterisation of α-amylase inhibitor from seeds of a wild variety of Lablab purpureus that show resistance to the bruchid Callosobruchus maculatusen_US
Appears in Collections: IJEB Vol.37(08) [August 1999]

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