Summary
Hypotonic human erythrocyte ghosts, devoid of the original glyceraldehyde-3-phosphate dehydrogenase content of the red cell, bind added glyceraldehyde-3-phosphate dehydrogenases, isolated from human erythrocytes, rabbit and pig muscle, as well as rabbit muscle aldolase. There are only slight differences in the affinities towards the various glyceraldehyde-3-phosphate dehydrogenases. On the other hand, glyceraldehyde-3-phosphate dehydrogenases are bound much stronger than aldolase; in an equimolar mixture the former can prevent the binding of the latter, or replace previously bound aldolase at the membrane surface. Binding is always accompanied by the partial inactivation of enzymes, which can be reverted by desorption. Unwashed ghosts rich in hemoglobin seem to have a more pronounced inactivating effect on bound glyceraldehyde-3-phosphate dehydrogenase. In isotonic media ghosts, whether white or unwashed, reseal and do not interact with the enzymes.
Similar content being viewed by others
References
Ács, G., Garzó, T., Grosz, G., Molnár, J., Stephaneck, O., and Straub, F. B., Acta Physiol. Acad. Sci. Hung. 8, 269–278, 1955.
McLaren, A. D. and Packe, L., Adv. Enzymol. 33, 245–308, 1970.
Gots, R. E. and Bessman, S. P., Arch. Biochem. Biophys. 163, 7–14, 1974.
Tanner, M. J. A. and Gray-, W. R., Biochem. J. 125, 1109–1117, 1971.
Carraway, K. L. and Shin, B. C., J. Biol. Chem. 247, 2102–2108, 1972.
Steck, T. L., Fairbanks, G., and Wallach, D. F. H., Biochemistry 10, 2617–2624, 1971.
Gourley, D. R. H., Arch. Biochem. Biophys. 40, 1–12, 1952.
Prankerd, T. A. J. and Altman, K. I., Biochem. J., 58, 622–633, 1954.
Schrier, S. L., Biochem. Biophys. Acta. 135, 691–698, 1967.
Latzkovits, L., Szentistványi, I., and Fajszi, Cs., Acta Biochem. Biophys. Acad. Sci. Hung. 7, 55–66, 1972.
Kant, J. A. and Steck, T. L., J. Biol. Chem. 248, 8457–8464, 1973.
Maretzki, D., Groth, J., Tsamaloukas, A. G., Gründel, M., Krüger, S., and Rapoport, S., FEBS Letters 39, 83–87, 1974.
Elödi, P. and Szörényi, E., Acta Physiol. Acad. Sci. Hung. 9, 339–350, 1956.
Taylor, J. F., Green, A. A., and Cori, G. T., J. Biol. Chem. 173, 591–604, 1948.
Jagannathan, V., Singh, K., and Damodaran, M., Biochem. J. 63, 94–105, 1956.
Friedrich, P., Arányi, P., and Nagy, I., Acta Biochem. Biophys. Acad. Sci. Hung. 7, 11–19, 1971.
Szewczuk, A., Wolny, M., Wolny, E., and Baranowski, T., Acta Biochim. Polon. 8, 201–207, 1961.
Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. J., J. Biol. Chem. 193, 265–275, 1951.
Biszku, E., Boross, L., and Szabolcsi, G., Acta Physiol. Acad. Sci. Hung. 25, 161–169, 1964.
Fox, J. B. and Dandliker, W. B., J. Biol. Chem. 221, 1005–1017, 1956.
Beutler, E., Red. Cell Metabolism, Grune and Stratton, New York, London, 1971.
Dodge, J. T., Mitchell, C., and Hanahan, D. J., Arch. Biochem. Biophys. 110, 119–130, 1963.
Fairbanks, G., Steck, T. L., and Wallach, D. F. H., Biochemistry 10, 2606–2616, 1971.
Weber, K. and Osborn, M., J. Biol. Chem. 244, 4406–4412, 1969.
Shin, B. C. and Carraway, K. L., J. Biol. Chem. 248, 1436–1444, 1973.
Arese, P., Bosia, A., Pesarmona, G. P., and Till, U., FEBS Letters 49, 33–36, 1974.
Mills, G. C. and Hill, F. L., Arch. Biochem. Biophys. 146, 306–311, 1971.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Solti, M., Friedrich, P. Partial reversible inactivation of enzymes due to binding to the human erythrocyte membrane. Mol Cell Biochem 10, 145–152 (1976). https://doi.org/10.1007/BF01731685
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF01731685