Purification and properties of a major isoform of beta-1,3-glucanase from pearl millet seedlings

Kini, K. R. and Vasanthi, N. S. and Umesh-Kumar, S. and Shetty, H. S. (2000) Purification and properties of a major isoform of beta-1,3-glucanase from pearl millet seedlings. Plant Science, 150 (2). pp. 139-145. ISSN 0168-9452

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Official URL: https://doi.org/10.1016/S0168-9452(99)00176-4

Abstract

A major isoform of beta-1,3-glucanase from pearl miller seedlings was purified following ammonium sulfate precipitation, ion-exchange chromatography and gel filtration techniques. The enzyme had a molecular weight of 20.5 kDa on SDS-PAGE and was highly basic with a pI of 9.6. It was thermostable with a broad temperature optima for activity ranging from 37 to 70 degrees C and had an optimum pH of 5.2. Mercuric chloride and para-chloromercuric benzoate inhibited completely the enzyme while manganese chloride activated it. Antibodies raised against the purified beta-1,3-glucanase identified another protein with an apparent molecular weight of 30 kDa in western reactions. Significance of this enzyme in pearl millet-downy mildew host-pathogen interaction is discussed. (C) 2000 Elsevier Science Ireland Ltd. All rights reserved.

Item Type: Article
Uncontrolled Keywords: beta-1,3-glucanase; pearl miller; downy mildew; host-pathogen interaction
Subjects: B Life Science > Biotechnology
Divisions: Department of > Biotechnology
Depositing User: Shrirekha N
Date Deposited: 25 Sep 2019 09:22
Last Modified: 25 Sep 2019 09:22
URI: http://eprints.uni-mysore.ac.in/id/eprint/8520

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