Abstract
Human superoxide dismutase A of the common phenotype SOD A1 is present in two electrophoretic forms in erythrocytes. These forms are charge isomers, easily permuting one into the other. Oxidation and reduction of the copper, partial or complete saturation of the dimers with copper, and presence of thiol groups on the enzyme do not seem to be involved.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Beckman, G. (1973). Population studies in northern Sweden. VI. Polymorphism of superoxide dismutase. Hereditas 73305.
Beckman, G., Lundgren, E., and Tarnvik, A. (1973). Superoxide dismutase isozymes in different human tissues, their genetic control and intracellular localization. Hum. Hered. 23338.
Calabrese, L., Federici, G., Bannister, W. H., Bannister, J. W., Rotilio, G., and Finazzi-Agrò, A. (1975). Labile sulfur in human superoxide dismutase. Eur. J. Biochem. 56305.
Carrico, R. J., and Deutsch, H. E. (1970). The presence of zinc in human cytocuprein and some properties of the apoprotein. J. Biol. Chem. 245723.
Fee, J. A. (1973). Studies on the reconstitution of bovine erythrocytes superoxide dismutase. Biochim. Biophys. Acta 295107.
Fee, J. A., and Dicorleto, P. E. (1973). Observation on the oxidation-reduction properties of bovine erythrocytes superoxide dismutase. Biochemistry 124893.
Ferguson, K. A. (1964). Starch gel electrophoresis: Applications to the classification of pituitary proteins and polyptides. Metabolism 13985.
Hedrick, J. L., and Smith, A. J. (1968). Size and charge isomer separation and estimation of molecular weights of proteins by disc-gel electrophoresis. Arch. Biochem. Biophys. 126155.
Marklund, S., Beckman, G., and Stigbrandt, T. (1976). A comparison between the common type and a rare genetic variant of human cupro-zinc superoxide dismutase. Eur. J. Biochem. 65415.
Morpurgo, L., Mavelli, I., Calabrese, L., Finazzi Agrò, A., and Rotilio, G. (1976). A ferrocyanide charge-transfer complex of bovine superoxide dismutase: Relevance of the zinc imidazolate bond to the redox properties of the enzyme. Biochem. Biophys. Res. Commun. 70607.
Rigo, A., Terenzi, M., Viglino, P., Calabrese, L., Cocco, D., and Rotilio, G. (1977). The binding of copper ions to copper-free bovine superoxide dismutase: Properties of the protein recombined with increasing amount of copper ions. Biochem. J. 16131.
Rotilio, G., Morpurgo, L., Calabrese, L., and Mondovì, B. (1973). On the mechanism of superoxide dismutase reaction of the bovine enzyme with hydrogen peroxide and ferrocyanide. Biochim. Biophys. Acta 302229.
Tegelstrom, H. (1975). Interspecific hybridisation in vitro of superoxide dismutase from various species. Hereditas 81185.
Weser, V., Barth, G., Vjerassi, C., Hartman, H. J., Krauss, P., Voelcker, G., Voelter, W., and Woetsch, W. (1972). A study on purified apo-erythrocuprein. Biochim. Biophys. Acta 27828.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Crosti, N. On the two electrophoretic forms of the Human superoxide dismutase A in the homozygote SOD A1. Biochem Genet 16, 739–742 (1978). https://doi.org/10.1007/BF00484730
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00484730