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Plant Physiology 65:834-837 (1980)
© 1980 American Society of Plant Biologists

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Partial Purification and Characterization of the mRNA for {alpha}-Amylase from Barley Aleurone Layers 1

Thomas J. Mozer2

Department of Biology, Washington University, St. Louis, Missouri 63130

The poly(A)-containing mRNA from barley aleurone layers pretreated with gibberellic acid has been purified by phenol-chloroform extraction and repeated oligo[d(pT)]-cellulose chromatography. This RNA has been translated in both the wheat germ and reticulocyte lysate in vitro translation systems with greater than 50% of the synthesized protein being {alpha}-amylase. The mRNA for {alpha}-amylase has been further purified by dimethylsulfoxide-formamide-sucrose density gradient centrifugation and by gel electrophoresis. By these methods, its molecular weight has been determined to be 580,000.


2 Present address: Monsanto Chemical Company, 800 North Lindbergh Blvd., St. Louis, Mo. 63166.

1 This work was supported by National Institutes of Health Postdoctoral fellowship 1-F32-GM06663-01, by a BRSG Grant awarded by the Biochemical Research Support Grant Program, Division of Research Resources, National Institutes of Health, by the Department of Biology, Faculty of Arts and Sciences Central Budget, Washington University, and by the Agricultural Products Division of Monsanto Chemical Company.




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J C Larkin, J P Hunsperger, D Culley, I Rubenstein, and C D Silflow
The organization and expression of a maize ribosomal protein gene family.
Genes & Dev., April 1, 1989; 3(4): 500 - 509.
[Abstract] [PDF]




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Copyright © 1980 by the American Society of Plant Biologists