Abstract
Protein patterns of four potato tuber varieties grown in the Northeastern United States were compared by electrophoresis and electrofocusing and found to be distinctly different. Molecular sizes of protein subunits of all four varieties were found to be uniform when charge differences between proteins were masked and disulfide bonds ruptured. Preliminary fractionation of Katahdin variety tuber proteins by dialysis against water yielded 25% globulin and 75% albumin. Further fractionation of the acidic proteins of the globulin fraction by density gradient isoelectric focusing at pH 4–6 separated three fractions isoelectric at pH 4.2, 4.4, and 5.3. Amino acid compositions of the three fractions were similar.
Resumen
Modelos de proteinas de 4 variedades de tubérculo de papa cultivadas en los estados del Noroeste fueron comparados por electroforesis y electroenfoque encontrándose que eran claramente diferentes. Los tamaños moleculares de las sub-unidades protéicas, de las cuatro variedades se encontraron uniformes cuando las diferencias de cargas entre las proteinas fueron encubiertas y los enlaces disulfitos rotos. Fraccionamiento preliminar de las proteinas de tubérculos de la variedad Katahdin mediante diálisis, con agua, rindió 25% de globulina y 75% de albúmina. Un mayor fraccionamiento de proteínas acídicas de la fracción globulina por gradientes de densidad con enfoque isoeléctrico a pH 4–6 separaron 3 fracciones isoeléctricas a pH 4.2, 4.4 y 5.3. La composición de aminoácidos de las tres fracciones fueron similares.
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Seibles, T.S. Studies on potato proteins. American Potato Journal 56, 415–425 (1979). https://doi.org/10.1007/BF02854059
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DOI: https://doi.org/10.1007/BF02854059