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Physiology and Biochemistry

Purification and Partial Characterization of Maize Dwarf Mosaic Virus Strain A. G. von Baumgarten, Graduate student, Plant Pathology Department, University of Illinois, Urbana 61801; R. E. Ford, professor, Plant Pathology Department, University of Illinois, Urbana 61801. Phytopathology 71:36-41. Accepted for publication 2 June 1980. Copyright 1981 The American Phytopathological Society. DOI: 10.1094/Phyto-71-36.

Maize dwarf mosaic virus strain A (M-A) was extracted by blending infected leaf tissue in pH 9.0 buffer, precipitating the virus with 4% polyethylene glycol (PEG) in 0.3 M NaCl, and purifying it by centrifugation in the rate-zonal or quasi-equilibrium gradients. Purity was determined by UV absorption spectra and gel electrophoresis. M-A yields from fresh infected tissue were 10–20 μg/g. Virus coat protein migrated as a single component in sodium dodecyl sulfate (SDS) polyacrylamide gels with apparent molecular weights of 30,700 or 35,500 from untreated or carboxymethylated preparations, respectively. A minimum molecular weight of 29,137 was determined by amino acid analysis based on seven histidine residues per subunit. Major differences in number of amino acid residues per subunit between M-A and M-B (maize dwarf mosaic virus strain B), respectively, were glutamic acid 37 and 29, glycine 18 and 34, lysine 22 and 12, serine 15 and 20, and threonine 19 and 25.

Additional keywords: protein, amino acids, polyacrylamide gel electrophoresis.