Abstract
Adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4) has been purified from human erythrocytes using a simple chromatographic procedure. Purified enzyme was obtained from individuals who were homozygous for the principal isozyme (ADA 1) as well as from individuals who were heterogyzous for the major variant (ADA 2-1). Although ADA 1 and ADA 2-1 are electrophoretically distinguishable, they have many common physical and catalytic properties. No significant differences between the two isozymic forms were found in measurements of molecular weight, catalytic activity in the presence of various substrates and inhibitors, pH optimum, turnover number, and stability in conditions of both high and low pH. ADA 2-1 was, however, substantially less stable than ADA 1 with respect to thermal denaturation. These studies support the idea that adenosine deaminase activity in erythrocytes is lower in those individuals who possess the variant form of the enzyme.
Similar content being viewed by others
References
György, P. and Rothler, H. 1927. Biochem. Z. 187: 194–219.
Agarwal, R. P., Sagar, S. M., and Parks, R. E., Jr. 1975. Biochem. Pharm. 24: 693–701.
Schrader, W. P., Stacy, A. R. and Pollara, B. 1976. J. Biol. Chem. 251: 4026–4032.
Daddona, P. E., and Kelley, W. N., 1977. J. Biol. Chem. 252: 6409–6415.
Berne, R. M., Rubio, R., and Curnish, R. R., 1974. Circ. Res. 35: 262–271.
Murray, A. W., 1971. Ann. Rev. Biochem. 40: 811–827.
Arch, J. R. S, and Newsholme, E. A., 1978. In Essays in Biochemistry, P. N. Campbell and W. N. Aldridge, eds., pp. 82–123, Vol. 14, Academic Press, New York.
Giblett, E. R., Anderson, J. E., Cohen, F., Pollara, B. and Menwissen, H. J., 1972. Lancet 2: 1067–1069.
Daddona, P. E. and Kelley, W. N., 1980. Mol. Cell. Biochem. 29: 91–101.
Hopkinson, D. A., Cook, P. J. L., and Harris, H., 1969. Ann. Hum. Genet. 32: 361–367.
Osborne, W. R. A., and Spencer, N., 1973. Biochem. J. 133: 117–123.
Edwards, Y. H., Hopkinson, D. A., and Harris, H., 1971. Ann. Hum. Genet., Lond. 35: 207–219.
Buel, E., and MacQuarrie, R. 1981. Prep. Biochem. 11: 363–380.
Körber, V., Meisterernst, E. B., Herman, G., 1975. Clinica Chim. Acta 63: 323–331.
Agarwal, R. P. and Parks, R. E., Jr., 1978. Meth. Enz. LI: 502–507.
Udenfriend, S., Stein, S., Bohlen, P., Dairman, W., Leimgruber, W., and Weigele, M., 1972. Sci. 178: 871–872.
Spencer, N., Hopkinson, D. A., and Harris, H., 1968. Ann. Hum. Genet., Lond. 32: 9–14.
Ma, P. F., Betras, S., and Dunnington, G., 1976. Anal. Biochem. 75: 177–182.
Agarwal, R. P., Spector, T., and Parks, R. E., Jr. 1977, Biochem. Pharm. 26: 359–367.
Cha, S., Agarwal, R. P., and Parks, R. E., Jr., 1975. Biochem. Pharm. 24: 2187–2197.
Battistuzzi, G., Scozzari, R., Santo Lanazza, P., Terrenato, L., and Modiano, G., 1974. Nature 251: 711.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
MacQuarrie, R., Buel, E. Physical and catalytic properties of the isozymes of adenosine deaminase from human red blood cells. Mol Cell Biochem 48, 121–126 (1982). https://doi.org/10.1007/BF00227611
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00227611