Variability in the concentration of three heat stable proteinase inhibitor proteins in potato tubers

Abstract

The variability of three well characterized proteinase inhibitors, Inhibitor I, molecular weight 39,000, Inhibitor II, molecular weight 21,000, and Carboxypeptidase Inhibitor, molecular weight 4,100, were determined in apical cortical tissues of individual potato tubers of the Russet Burbank variety. The three inhibitors varied within ± 20% among sixty-five tubers and cumulatively represented about 7% of the total soluble proteins. The inhibitors were highly variable among tubers of 106 clones from randomly chosen varieties. Inhibitor I varied about twelve-fold (60 to 745 μg/ml juice), and Inhibitor II varied about seven-fold (158 to 1,025 μg/ml juice). Carboxypeptidase Inhibitor varied from as low as zero (seven varieties) to over 850 μg/ml tuber juice. With 80 tubers from fourteen varieties of potatoes, a positivecorrelation was found between the concentrations of Inhibitor I and Inhibitor II and total soluble protein. Carboxypeptidase Inhibitor did not correlate well with total soluble protein. The positive correlations of Inhibitors I and II (a correlation coefficient of 0.70) with total soluble protein indicated that the proteinase inhibitors may be excellent markers for genetic studies for selecting high protein potato tuber varieties. © 1976 Springer.