Analysis ofl-alanine:2-oxoglutarate aminotransferase isozymes in maize |
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| Authors: | Nancy R Watson Virginia M Peschke Douglas A Russell Martin M Sachs |
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| Institution: | (1) Department of Biology, Washington University, 63130 St. Louis, Missouri;(2) Department of Agronomy, Turner Hall, University of Illinois, 61801 Urbana, Illinois;(3) Present address: Makhethisa Sec. School, P.O. Box 408, 300 Leribe, Lesotho;(4) Present address: Plant Sciences, Monsanto Company, 700 Chesterfield Village Parkway, 63198 St. Louis, Missouri |
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| Abstract: | Isozyme analysis ofl-alanine:2-oxoglutarate aminotransferase (ALT) in maize indicates that there are three genes encoding this enzyme activity. Two of the gene products interact with each other to form heterodimers, while the third gene product does not interact with the other two. Another isozyme that appears after gel electrophoresis and ALT staining is shown to be glutamate dehydrogenase-1. Anaerobic treatment does not result in increased ALT levels, indicating that the previously reported increase in alanine levels caused by this treatment may be due to increases in the level of pyruvate, a substrate of ALT.D. A. Russell was partially supported by a graduate student fellowship from the Division of Biology and Biomedical Sciences, Washington University. V. M. Peschke was partially supported by a postdoctoral fellowship from Monsanto. This research was supported by NIH Grant R01 GM34740. |
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| Keywords: | alanine aminotransferase maize isozymes allozymes glutamate dehydrogenase |
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