Purification and characterization of an anaerobically induced alanine aminotransferase from barley roots
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Good, A.G., & Muench, D. G. (1992). Purification and characterization of an anaerobically induced alanine aminotransferase from barley roots. Plant Physiology, 99, 1520-1525. DOI: 10.1104/pp.99.4.1520.
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Abstract
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Alanine aminotransferase (AlaAT, EC 2.6.1.2) is an enzyme that is induced under anaerobic conditions in cereal roots. In barley (Hordeum vulgare L.) roots, there are a number of isoforms of AlaAT. We have identified the anaerobically induced isoform and have purified it to homogeneity. The isolation procedure involved a two-step ammonium sulfate precipitation, gel filtration, ion-exchange chromatography, and chromatofocusing. The enzyme was purified approximately 350-fold to a specific activity of 2231 units/milligram protein. The apparent molecular masses of the native and sodium dodecyl sulfate-denatured AlaAT proteins are 97 and 50 kilodaltons, respectively, indicating that the native enzyme is probably a homodimer. AlaAT has a number of interesting characteristics when compared with other plant aminotransferases. AlaAT does not require the presence of pyridoxyl-5-phosphate to retain its activity, and it appears to be very specific in the reactions that it will catalyze.
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http://purl.org/coar/resource_type/c_6501 http://purl.org/coar/version/c_970fb48d4fbd8a85
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© 1992 American Society of Plant Biologists. This version of this article is open access and can be downloaded and shared. The original author(s) and source must be cited.
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en