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The Saginaw and Sanilac varieties of navy beans (Phaseolus vulgaris L.), were utilized. The former is tolerant and the latter is extremely sensitive to both zinc deficiency and excessive levels of zinc. Electrophoretic patterns of the water-soluble leaf proteins revealed a slowmoving, major band, the change in intensity of which clearly reflected a differential zinc response of the two varieties. There was a moderate decrease in band intensity under low zinc for the tolerant Saginaw, with astriking depression for the sensitive Sanilac. This protein band, with a relative electrophoretic mobility of 0.11 in 7% polyacrylamide gel at pH 8.9, was tentatively identified as Fraction I protein which is reported to contain ribulose diphosphate carboxylase, the enzyme primarily responsible for photosynthetic carbon dioxide fixation in many plants. Fraction I protein, zinc nutrition, and the differential response of Saginaw and Sanilac plants to zinc were correlated.
Key Words: Navy beans Zinc deficiency Protein Gel electrophoresis
2 Department of Biology, University of Toledo, Toledo, Ohio 43606.
3 Departments of Crop Science and Horticulture, Michigan State University, East Lansing, Mich 48823 (Polson is now Assistant Professor, Department of Agronomy and Plant Genetics, University of Minnesota, St. Paul, Minn. 55101.
Received for publication May 22, 1971.
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