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This article in CS

  1. Vol. 12 No. 1, p. 26-29
    Received: May 22, 1971

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Differential Response to Two Bean Varieties to Zinc as Revealed by Electrophoretic Protein Pattern1

  1. W. H. Jyung2,
  2. M. E. Camp2,
  3. D. E. Polson3,
  4. M. W. Adams3 and
  5. S. H. Wittwer3



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.

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