Abstract
The regulation of adenosine metabolism is an important factor in the determination of the biological properties of this compoundl. Although the deamination of adenosine has been carefully characterized, only a limited amount of information is available concerning its phosphorylation in mammalian tissue. We have undertaken the purification and characterization of human placental adenosine kinase (E. C.2.7.1.20), which catalyzes the reaction:
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References
I. H. Fox and W. N. Kelley, The role of adenosine and deoxyadenosine in mammalian cells, Ann. Rev. Biochem. 47:655 (1978).
C.M. Andres and I. H. Fox, The phosphorylation of adenosine and deoxyadenosine using purified adenosine kinase, Clin. Res. 26:671A (1978).
C.M. Andres and I. H. Fox, Purification and properties of human placental adenosine kinase, (In Preparation).
T. D. Palella, C. M. Andres, and I. H. Fox, Regulation of human placental adenosine kinase, Fed. Proc. 38:669 (1979).
T. D. Palella, C. M. Andres, and I. H. Fox, Regulation of human placental adenosine kinase, (In Preparation).
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© 1980 Plenum Press, New York
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Andres, C.M., Palella, T.D., Fox, I.H. (1980). Human Placental Adenosine Kinase: Purification and Characterization. In: Rapado, A., Watts, R.W.E., De Bruyn, C.H.M.M. (eds) Purine Metabolism in Man—III. Advances in Experimental Medicine and Biology, vol 122B. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8559-2_8
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DOI: https://doi.org/10.1007/978-1-4684-8559-2_8
Publisher Name: Springer, Boston, MA
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