American Potato Journal

, Volume 53, Issue 12, pp 443–455 | Cite as

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

  • C. A. Ryan
  • T. Kuo
  • G. Pearce
  • R. Kunkel


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.


Potato Tuber AMERICAN Potato Journal Total Soluble Protein Russet Burbank Potato Potato Clone 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


La variabilidad de tres inhibidores de proteínasa bien caracterizados, Inhibidor I, 39,000 de peso molecular, Inhibidor II, 21,000 de peso molecular y un Inhibidor de carboxypeptidasa, 4100 de peso molecular, fueron determinados en tejido cortical del ápice de tubérculos individuates de papa de la variedad Russet Burbank. Los tres inhibidores variaron dentro ±20% entre sesenta y cinco tubeŕculos y acumulativamente representaron aproximadamente 7% de las proteínas solubles totales. Los inhibidores fueron muy variables entre los tubérculos de 106 clones de muestras escogidas al azar. El Inhibidor I varió alrededor de doce veces (60 a 745 μg/ml de judo) y el Inhibidor II varió aproximadamente siete veces (158 a 1025 μg/ml de jugo). El Inhibidor de carboxypeptidasa varió desde valores tan bajo como cero (siete variedades) a por encima de 850 μg/ml de jugo de tubérculos. Con 80 tubérculos de 14 variedades de papa, se encontró una correlación positiva entre las concentraciones del Inhibidor I y del Inhibidor II y la proteína soluble total. El Inhibidor de carboxypeptidasa no correlacioné bien con la proteina soluble total. Las correlaciones positivas de los inhibidores I y II (un coeficiente de correlación de 0.70) con la proteína soluble total indicó que los inhibidores de proteinasa pueden ser excelentes parámetras para los estudios de génetica en la selección de variedades de papa con alta proteína en el tubérculo.


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Literature Cited

  1. 1.
    Belitz, H.-D., Kaiser, K.-P., and Santarius, K. 1971. Trypsin and Chymotrypsin Inhibitors from Potatoes: Isolation and Some Properties. Biochem Biophys Res Commun 42:420–427.PubMedCrossRefGoogle Scholar
  2. 2.
    Bryant, J., Green, T.R., Gurusaddaiah, T., and Ryan, C.A. Proteinase Inhibitor II from Potatoes. Isolation and Characterization of its Subunit Components. Biochemistry in Press.Google Scholar
  3. 3.
    Haas, G.M., Nau, H., Biemann, K., Grahn, T.D., Ericksson, L.H., and Neurath, H. 1975. The Amino Acid Sequence of a Carboxypeptidase Inhibitor from Potatoes. Biochemistry 14:1334–1342.CrossRefGoogle Scholar
  4. 4.
    Hochstrasser, K., Werle, E. 1969. Isolation and Characterization of a Polyvalent Proteinase Inhibitor fromSolarium tuberosum. Hoppe-Seyler’s Z Physiol Chem 350:897–902.PubMedGoogle Scholar
  5. 5.
    Hoff, J.E., Jones, C.M., Sosa, M.P., and Rodis, P. 1972. Naturally Occurring Crystals in the Potato: Isolation and Identification as a Protein. Biochem Biophys Res Commun 49:1525–1527.PubMedCrossRefGoogle Scholar
  6. 6.
    Hojima, Y., Moriya, H., and Moriwaki, C. 1973. Studies of Kallikrein Inhibitors from Potatoes. J Biochem (Tokyo) 73:923–932.Google Scholar
  7. 7.
    Hughes, B.P. 1958. The Amino Acid Composition of Potato Protein and of Cooked Potato. Br JNutr 12:188.CrossRefGoogle Scholar
  8. 8.
    Iwasaki, T., Kiyohara, T., and Yoshikawa, M. 1972. Chemical and Physicochemical Characterization of Two Different Types of Proteinase Inhibitors (Inhibitors Ha and IIb) from Potatoes. J Biochem (Tokyo) 72:1029–1035.Google Scholar
  9. 9.
    Kaiser, K.-P., and Belitz, H.-D. 1972. Proteinase Inhibitors. VI. Some Properties of Various Trypsin and Chymotrypsin Inhibitors from Potatoes. Chem Mikrobiol Technol Lebensm 1:191–194.Google Scholar
  10. 10.
    Kiyohara, T., Iwasaki, T., and Yoshikawa, M. 1973. Chemical and Physicochemical Properties of Potato Proteinase Inhibitor I and Comparison of Its Specificity with Those of Inhibitors IIa and IIb. J Biochem (Tokyo) 73:89–95.Google Scholar
  11. 11.
    Laskowski, M., Jr., and Sealock, R.W. 1971 Protein Proteinase “The Enzymes”, P. Boyer, Editor. Academic Press pp. 375–473.Google Scholar
  12. 12.
    Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. 1951. Protein Measurement with the Folin-phenol Reagent. J Biol Chem 193:265–290.PubMedGoogle Scholar
  13. 13.
    Melville, J.C., and Ryan, C. A. 1972. Chymotrypsin Inhibitor I from Potatoes. J Biol Chem 247: 3445–3453.PubMedGoogle Scholar
  14. 14.
    Ryan, C.A. 1966. Chymotrypsin Inhibitor I from Potatoes: Reactivity with Mammalian, Plant, Bacterial, and Fungal Proteinases. Biochemistry 5:1592–1596.PubMedCrossRefGoogle Scholar
  15. 15.
    Ryan, C.A. 1967. Quantitative Determination of Soluble Cellular Proteins by Radial Diffusion in Agar Gels Containing Antibodies. Anal Biochem 19:434–440.PubMedCrossRefGoogle Scholar
  16. 16.
    Ryan, C.A. 1973. Proteolytic Enzymes and Their Inhibitors in Plants. Annu Rev Plant Physiol 24:173–196.CrossRefGoogle Scholar
  17. 17.
    Ryan, C.A., and Balls, A.K. 1962. An Inhibitor of Chymotrypsin fromSolanum tuberosum and its Behavior Toward Trypsin. Proc Natl. Acad Sci USA 48:1839–1844.PubMedCrossRefGoogle Scholar
  18. 18.
    Ryan, C.A., Haas, G.M.,and Kuhn, R. 1974. Purification and Properties of a Carboxypeptidase Inhibitor from Potatoes. J Biol Chem 249:5495–5499.PubMedGoogle Scholar
  19. 19.
    Rouleau, M., and Lamy, F. 1975. Purification and Characterization of aTrypsin Inhibitor fromSolanum tuberosum. Can J Biochem 53:958–974.PubMedCrossRefGoogle Scholar
  20. 20.
    Santarius, K., and Belitz, H.-D. 1972. Proteinase Inhibitors. V. Isolation and Some Properties of Inhibitor A5 from Potatoes. Chem Mikrobiol Technol Lebensm 2:56–62.Google Scholar
  21. 21.
    Sawada, J., Yasui, H., Amamoto, T., Yamada, M., Okazaki, T., and Tanaka, I. 1974. Isolation and Some Properties of Anti-Proteolytic Polypeptides from Potato. Agric Biol Chem 38:2559–2561.Google Scholar
  22. 22.
    Solyom, A., Borsy, J., and Tolnay, P. 1964. Elastase Inhibitors of Plant Origin. Biochem Pharmacol 13:391–394.PubMedCrossRefGoogle Scholar
  23. 23.
    Steyermark, A. 1951. Quantitative Organic Microanalysis. The Blakeston Co., New York, pp. 134–155.Google Scholar
  24. 24.
    Trautman, R., Cowan, K.M., and Wagner, G.G. 1971. Data Processing for Radial Immunodiffusion. Immunochemistry 8:901–916.PubMedCrossRefGoogle Scholar
  25. 25.
    Worowski, K. 1974. An Antiproteolytic and Antifibrinolysis Preparation Obtained from Potato by Means of Chromatography on SE-Sephadex G50. Thromb Diath Haemorrh 32:617–631.PubMedGoogle Scholar

Copyright information

© Springer 1976

Authors and Affiliations

  • C. A. Ryan
    • 1
    • 2
  • T. Kuo
    • 1
    • 2
  • G. Pearce
    • 1
    • 2
  • R. Kunkel
    • 1
    • 2
  1. 1.Department of Agricultural Chemistry, Program in Biochemistry and Biophysics Department of HorticultureWashington State UniversityPullman
  2. 2.Department of HorticultureWashington State UniversityPullman

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