Abstract
The search for specific enzymatic reactions which can clearly differentiate normal mammalian cells from both malignant cells and infective microorganisms represents a major strategy for the development of selective therapeutical approaches. In particular, the intensive research carried out in the past on purine and pyrimidine metabolism has yielded a very rich harvest of drugs effective in the treatment of malignancy as well as of parasitic diseases.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
N. Kamatani and D.A. Carson, Dependence of adenine production upon polyamine synthesis in cultured human lymphoblasts, Biochim. Biophys. Acta 675: 344 (1983)
J.A. Duerre, A hydrolytic nucleosidase acting on S-adenosylhomocysteine and on 5′-methylthioadenosine, J. Biol. Chem. 237: 3737 (1962)
F. Della Ragione, M. Porcelli, M. Cartenì-Farina, V. Zappia, A.E. Pegg, Escherichia coli S-adenosylhomocysteine/5′-methylthioadenosine nucleosidase: purification, substrate specificity and mechanism of action, Biochem. J. 232: 335 (1985)
Y. Sugimoto, T. Toraya and S. Fukui, Studies on metabolic role of 5′-methylthioadenosine in Ochromonas malhamensis and other microorganisms, Arch. Microbiol. 108: 175 (1976)
C. Baxter and C.J. Coscia, In vitro synthesis of spermidine in the higher plant, Vinca rosea, Biochem. Biophys. Res. Commun. 59: 147 (1973)
A.B. Guranowski, P.K. Chiang and G.L. Cantoni, 5′-Methylthioadenosine nucleosidase: purification and characterization of the enzyme from Lupinus luteus seeds, Eur. J. Biochem. 114: 243 (1981)
A.E. Pegg and H.G. Williams-Ashman, Phosphate-stimulated breakdown of 5′-methylthioadenosine by rat ventral prostate, Biochem. J. 115: 241 (1969)
D.L. Garbers, Demonstration of 5′-methylthioadenosine phosphorylase activity in various rat tissues: some properties of the enzyme from rat lung, Biochim. Biophys. Acta, 523: 82 (1978)
V. Zappia, A. Oliva, G. Cacciapuoti, P. Galletti, G. Mignucci and M. Cartenì-Farina, Substrate specificity of 5′-methylthioadenosine phosphorylase from human prostate, Biochem. J. 175: 1043 (1978)
G. Cacciapuoti, A. Oliva and V. Zappia, Studies on phosphate-activated 5′-methylthioadenosine nucleosidase from human placenta, Int. J. Biochem. 9: 35 (1978)
T.M. Savarese, G.W. Crabtree and R.E. Parks Jr, 5′-Methylthioadenosine phosphorylase — I: substrate activity of 5′-deoxyadenosine with the enzyme from sarcoma 180 cells, Biochem. Pharmacol. 30: 189 (1981)
A.J. Ferro, N.C. Wobei and J.A. Nicolette, 5-Methylthioribose-1-phosphate: a. product of partially purified rat liver 5′-methylthioadenosine phosphorylase, Biochim. Biophys. Acta 570: 65 (1979)
L. Shugart, M. Tancer and J. Moore, Methylthioadenosine nucleoside phosphorylase activity in Drosophila melanogaster, Int. J. Biochem. 10: 901 (1979)
S. Shimizu, T. Abe, S. Shiozaki and H. Yamada, Catabolism of methylthioadenosine and S-adenosylhomocysteine in microorganisms, in International Conference on Polyamines in Life Sciences, Lake Yamanaka, Japan, July 14–18 (1986)
R.L. Miller, C.L.K. Sabourin and T.A. Krenitsky, Trypanosoma cruzi adenine nucleoside phosphorylase purification and substrate specificity, Biochem. Pharmacol. 36: 553 (1987)
N. Kamatani, W.A. Nelson-Rees and D.A. Carson, Selective killing of human malignant cells deficient in methylthioadenosine phosphorylase, a purine metabolic enzyme, Proc. Natl. Acad. Sci. USA 78: 1219 (1981)
T.M. Savarese, S-H. Chu, M-Y Chu and R.E. Parks Jr, 5′-Deoxy-5′-methylthioadenosine phosphorylase-III: role of the enzyme in the metabolism and action of 5′-halogenated adenosine analogs, Biochem. Pharmacol. 34: 361 (1985)
P.S. Backlund and R.A. Smith, Methionine synthesis from 5′-methylthioadenosine in rat liver, J. Biol. Chem. 256: 1533 (1981)
F. Della Ragione, M. Cartenì-Farina, V. Gragnaniello, M.I. Schettino and V. Zappia, Purification and characterization of 5′-deoxy-5′-methylthioadenosine phosphorylase from human placenta, J. Biol. Chem. 261: 12324 (1986)
J.D. Stoeckler, R.P. Agarwal, K.C. Agarwal, K. Schmid and R.E. Parks Jr, Purine nucleoside phosphorylase from human erythrocytes: physicochemical properties of the crystalline enzyme, Biochemistry 17: 278 (1978)
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1988 Plenum Press, New York
About this chapter
Cite this chapter
Ragione, F.D., Oliva, A., Fioretti, M., Russo, G.L., Palumbo, R., Zappia, V. (1988). Physico-Chemical and Immunological Properties of Bovine Liver 5′-Deoxy-5′-Methylthioadenosine Phosphorylase. In: Zappia, V., Pegg, A.E. (eds) Progress in Polyamine Research. Advances in Experimental Medicine and Biology, vol 250. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5637-0_17
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5637-0_17
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5639-4
Online ISBN: 978-1-4684-5637-0
eBook Packages: Springer Book Archive