Summary
Soluble cyclic nucleotide 3′:5′ monophosphate phosphodiesterase (PDE) (EC 3.1.4.17) obtained from beef adrenal cortex as the 100,000 g/1.5 h supernatant is usually regarded as a very hydrophilic protein. However, when subjected to hydrophobic chromatography on Octyl-Sepharose CL 413 it reveals strong hydrophobic interaction with the column matrix. The chromatographic procedure leads to multiple but distinct forms of PDE which degrade cAMP beyond 5′AMP to inosine, via adenosine. The same metabolic pathway was previously observed with a membrane bound multienzyme sequence. Even the soluble PDE forms separated by gel chromatography (Sephadex G 200, Sepharose S 200 and Sepharose 6B) and soluble PDE of other tissue (heart) displayed the same metabolic pattern. These findings indicate a linkage between PDE, nucleotidase and deaminase activities. The intimate association of the enzyme is additionally supported by the phenomenon of “kinetic advantage” clearly observed with the most hydrophobic PDE form. Its end product, inosine, is formed more rapidly from CAMP than from the intermediate 5′AMP. This paradoxical phenomenon is explained by close physical proximity between the enzymes involved in the metabolic pathway. Furthermore, when the most hydrophobic PDE form was immobilized on Octyl-Sepharose, rather than loss of catalytic activity even higher enzyme activities were measured. It is suggested that the so-called multiple forms of soluble PDE-at least in part-represent more or less preserved forms of a native, membrane bound, multienzyme sequence which degrades cyclic nucleotides.
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References
Drummond, G. I. and Perrott-Yee, S., 1961. J. Biol. Chem. 236, 1126–1129.
Nair, K. G., 1965. Biochemistry 5, 150–157.
DeRobertis, E., Arnaiz, G. R. D. I., Alberici, A., Butcher, R. W. and Sutherland, E. W., 1967. J. Biol. Chem. 242, 3487–3493.
Butcher, R. W. and Sutherland, E. W., 1962. J. Biol. Chem. 237, 1244–1250.
Cheung, W. Y. and Salganicoff, L., 1967. Nature 214, 90–91.
Wombacher, H., 1980, Arch. Biochem. Biophys. (in the press).
Cheung, W. Y., 1970. In Advan. in Biochem. Psychopharmacology (ed. Greengard, P. and Costa, E.) Vol. 3 Role of cyclic AMP in Cell Function pp. 51–65, Raven Press. New York.
Wells, J. N. and Hardman, J. G., 1977. In “Advances in Cyclic Nucleotide Research” (ed. Greengrad, P. and Robison, G. A.) Vol. 8, pp. 119–143, Raven Press, New York.
Reuter-Smerdka, M. and Wombacher, H., 1978. 12th FEBS Meeting, Dresden, Abstract No.: 1257.
Wombacher, H., 1978. 12th FEBS Meeting, Dresden, Abstract No.: 1258.
Wombacher. H., 1978. FEBS Lett. 85, 77–80.
Peter, H. W. and Wolf, H. U., 1973. J. Chromat. 82, 15–30.
Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J., 1951. J. Biol. Chem. 193, 265–275.
von der Haar, F., 1978. In “Theory and Practice in Affinity Techniques” (ed. Sundaram, P. V. and Eckstein, F.) p. 1–13 Academic Press, London, New York, San Francisco.
Wilchek, M. and Miron, T., 1976. Biochem. Biophys. Res. Commun. 72, 108–113.
King, T. P., 1972. Biochemistry, 11, 367–371.
von der Haar, F., 1976. Biochem. Biophys. Res. Commun. 70, 1009–1013.
Pichard, A. L. and Cheung, W. Y., 1977. J. Biol. Chem. 252, 4872–4875.
Cheung, W. Y., 1970. Biochem. Biophys. Res. Commun. 38, 533–538.
Cheung, W. Y., 1971. J. Biol. Chem. 246, 2858–2869.
Kakiuchi, S., Yamazaki, R. and Nakajima, H., 1970. Proc. Jap. Acad. 46, 587–592.
Dumler, I. L. and Etingof, R. N., 1976. Biochem. Biophys. Acta 429, 474–484.
Wang, J. H. and Desai, R., 1976. Biochem. Biophys. Res. Commun. 72, 926–932.
Ho, R. J., Russel, T. R., Asakawa, T. and Hucks, M. W., 1975. J. Cyclic Nucl. Res. 1, 81–88.
Filburn, C. R. and Sacktor, B., 1976. Arch. Biochem. Biophys. 174, 249–261.
Strada, S. J. and Thompson, W. J., 1978. In “Advances in Cyclic Nucleotide Research” (ed. George, W. J. and Ignarro, D. J.) Vol. 9 pp. 265–283, Raven Press, New York.
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Wombacher, H. Hydrophobic interaction of soluble 3′:5′ cyclic nucleotide phosphodiesterase with octyl-sepharose. Mol Cell Biochem 30, 157–164 (1980). https://doi.org/10.1007/BF00230169
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DOI: https://doi.org/10.1007/BF00230169