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Ascochyta Rabiei

pathogenesis-related protein prompted by disease with Ascochyta rabiei was segregated from intercellular washing liquid of chickpea (Cicer arietinum L.) leaves. The amino-terminal arrangement of the protein was common of a thaumatin-like protein (TLP). The isoelectric point was 6.5 and the atomic mass was 16 kDa; consequently, chickpea PR-5a is a little TLP. PR-5a needed antifungal movement toward A. rabiei. Screening of a chickpea reciprocal DNA (cDNA) library brought about segregation of a cDNA clone (p5a-241) for this protein. A subsequent cDNA clone (ELR112) encoding a TLP was confined utilizing differential hybridization of cDNA libraries got from inspired and water-rewarded cell suspension societies of chickpea. The found protein (PR-5b) had a sub-atomic mass of 22 kDa. PR-5b was limited in the vacuole inferable from the nearness of an individual N-terminal sign peptide and a carboxy-terminal expansion. Southern smear investigations uncovered that ELR112 and p5a-241 spoke to single-duplicate qualities. During parasitic disease of chickpea plants, articulation of the two qualities continued a lot quicker in an A.  

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BioTechnology: An Indian Journal received 875 citations as per Google Scholar report

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