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Purification of Two Basic 1, 3-b-Glucanase Isoforms from Cyamopsis tetragonoloba (L.)Taub. Induced to Resist Virus Infections

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1,3-b-glucanases (EC are enzymes that degrade polysaccharidic substratesand have antimicrobial activity against fungi and bacteria. They have also been implicated in systemic acquired resistance (SAR) indirectly through release of endogenous elicitor molecules. SAR against viruses can be induced in plants by a few substances, including proteins isolated from some non-host plants. In the present study, CAP-34, a 34 kDa basic protein isolated from Clerodendrumaculeatum L., was used to induce systemic resistance against sunnhemp rosette virusin Cyamopsis tetragonoloba (L.) Taub. 1,3-b-glucanase activity increased rapidlyfollowing treatment with CAP-34. The glucanase induction started within 3 h oftreatment, and maintained a peak value between 6 and 24 h before declining between48 and 72 h. Two isoforms were purified from resistant C. tetragonoloba. Both were basic and possessed an Mr of 34 and 36 kDa. Their pI was greater than pH 9.3. p Hoptima were 5.5 and 5.6 for the 34 and 36 kDa isoforms, respectively, while their K mwas 400 and 666.6mg ml–1. While the total yield of the 36 kDa glucanase was considerably higher than the 34 kDa isoform, its specific activity was less.

Affiliations: 1: Department of Botany, University of Lucknow


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