Summary
Oxygen was found to sensitize the radiation-induced deactivation of immobilizedα-chymotrypsin but protected the free enzyme in solution. In the system with immobilized enzyme, radiation-induced enzyme deactivation can only occur in the small volume element where the enzyme is located. Oxygen should therefore reduce radical recombination outside this volume element, resulting in an increased number of radical (⋅ OH, ⋅ O− 2, ⋅ HO2)-immobilized enzyme reactions. The results then indicate that most of the solvent radicals are terminated within 50 Å from the point of origin.
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References
Anbar, M., Neta, P.: Intern. J. Appl. Radiation and Isotopes18, 493 (1967)
Chandrasekar, S.: Stochastic problems in physics and astronomy. Rev. Mod. Physics15, 1, 89 (1943)
Dertinger, H., Jung, H.: Molekulare Strahlenbiologie, p. 46. Berlin-Heidelberg-New York: Springer 1969
Gabel, D., Steinberg, I. Z., Katchalski, E.: Changes in conformation of insolubilized trypsin and chymotrypsin followed by fluorescence. Biochemistry10, 4661–4669 (1971)
Howard-Flanders, P., Alper, T.: The sensitivity of microorganisms to irradiation under controlled gas conditions. Radiation Research7, 518–529 (1957)
Hutchinson, F.: The distance that a radical formed by ionizing radiation can diffuse in a yeast cell. Radiation Research7, 473–883 (1957)
Kasche, V., Lundqvist, H., Bergman, R., Axen, R.: A theoretical model describing steady-state catalysis by enzymes immobilized in spherical gel particles. Experimental study ofα-chymotrypsin-Sepharose. Biochem. Biophys. Res. Comm.45, 615–621 (1971)
Kasche, V.: Specific protein-protein interaction and its application in studies on radiation-induced protein modification. Acta Universitas Upsaliensis2, 1–132 (1971)
Kasche, V.: Effects of the microenvironment of the specific interaction betweenα-chymotrypsin and immobilized soybean trypsin inhibitor. Studia biophysica35, 45 (1973)
Matthews, B. W., Sigler, P. B., Henderson, R., Blow, D. M.: Three-dimensional structure of tosyl-α-chymotrypsin. Nature214, 652–656 (1967)
Porath, J., Janson, J.-C., Låås, T.: Agar derivatives for chromatography, electrophoresis and gel-bound enzymes. J. Chromatogr.60, 167–177 (1971)
Renkin, E.: Filtration, diffusion, and molecular sieving through porous cellulose membranes. J. Gen. Physiol.38, 225–243 (1954)
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Supported by grants 184-14 and 184-15 from the Swedish Atomic Research Council.
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Kasche, V. Oxygen effect: Differences in radiation-induced deactivation of mobile and immobilizedα-chymotrypsin. Radiat Environ Biophys 11, 189–193 (1974). https://doi.org/10.1007/BF01323186
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DOI: https://doi.org/10.1007/BF01323186