Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1984 May 15;220(1):269–272. doi: 10.1042/bj2200269

Properties of extracellular superoxide dismutase from human lung.

S L Marklund
PMCID: PMC1153619  PMID: 6331409

Abstract

A further characterization of human extracellular superoxide dismutase is reported. The study was especially aimed at the interaction with substances known to interfere with CuZn superoxide dismutase and other superoxide dismutases. Extracellular superoxide dismutase is efficiently inhibited by cyanide and is about 3 times more sensitive than is human CuZn superoxide dismutase. The sensitivity to azide is much lower, but still about 3 times higher than that of human CuZn superoxide dismutase. Extracellular superoxide dismutase is about as rapidly inactivated by hydrogen peroxide as is CuZn superoxide dismutase. The sensitivity to diethyldithiocarbamate is very high and more than an order of magnitude larger than that of CuZn superoxide dismutase. Sodium dodecyl sulphate, under conditions suggested as being suitable for distinguishing between the insensitive CuZn superoxide dismutase and the sensitive Mn superoxide dismutase, efficiently inactivated extracellular superoxide dismutase. No antigenic similarities between extracellular superoxide dismutase and CuZn superoxide dismutase could be demonstrated. Anti-(extracellular superoxide dismutase) did not bind CuZn superoxide dismutase, and anti-(CuZn superoxide dismutase) did not bind extracellular superoxide dismutase.

Full text

PDF
270

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Beauchamp C. O., Fridovich I. Isozymes of superoxide dismutase from wheat germ. Biochim Biophys Acta. 1973 Jul 12;317(1):50–64. doi: 10.1016/0005-2795(73)90198-0. [DOI] [PubMed] [Google Scholar]
  2. Blech D. M., Borders C. L., Jr Hydroperoxide anion, HO-2, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: modification of one histidine per subunit. Arch Biochem Biophys. 1983 Jul 15;224(2):579–586. doi: 10.1016/0003-9861(83)90245-x. [DOI] [PubMed] [Google Scholar]
  3. Bray R. C., Cockle S. A., Fielden E. M., Roberts P. B., Rotilio G., Calabrese L. Reduction and inactivation of superoxide dismutase by hydrogen peroxide. Biochem J. 1974 Apr;139(1):43–48. doi: 10.1042/bj1390043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cocco D., Calabrese L., Rigo A., Argese E., Rotilio G. Re-examination of the reaction of diethyldithiocarbamate with the copper of superoxide dismutase. J Biol Chem. 1981 Sep 10;256(17):8983–8986. [PubMed] [Google Scholar]
  5. Crapo J. D., McCord J. M., Fridovich I. Preparation and assay of superoxide dismutases. Methods Enzymol. 1978;53:382–393. doi: 10.1016/s0076-6879(78)53044-9. [DOI] [PubMed] [Google Scholar]
  6. Geller B. L., Winge D. R. A method for distinguishing Cu,Zn- and Mn-containing superoxide dismutases. Anal Biochem. 1983 Jan;128(1):86–92. doi: 10.1016/0003-2697(83)90348-2. [DOI] [PubMed] [Google Scholar]
  7. Heikkila R. E., Cabbat F. S., Cohen G. In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate. J Biol Chem. 1976 Apr 10;251(7):2182–2185. [PubMed] [Google Scholar]
  8. Hodgson E. K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry. 1975 Dec 2;14(24):5294–5299. doi: 10.1021/bi00695a010. [DOI] [PubMed] [Google Scholar]
  9. Keele B. B., Jr, McCord J. M., Fridovich I. Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme. J Biol Chem. 1970 Nov 25;245(22):6176–6181. [PubMed] [Google Scholar]
  10. Marklund S. L., Holme E., Hellner L. Superoxide dismutase in extracellular fluids. Clin Chim Acta. 1982 Nov 24;126(1):41–51. doi: 10.1016/0009-8981(82)90360-6. [DOI] [PubMed] [Google Scholar]
  11. Marklund S. L. Human copper-containing superoxide dismutase of high molecular weight. Proc Natl Acad Sci U S A. 1982 Dec;79(24):7634–7638. doi: 10.1073/pnas.79.24.7634. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Marklund S., Beckman G., Stigbrand T. A comparison between the common type and a rare genetic variant of human cupro-zinc superoxide dismutase. Eur J Biochem. 1976 Jun 1;65(2):415–422. doi: 10.1111/j.1432-1033.1976.tb10356.x. [DOI] [PubMed] [Google Scholar]
  13. Marklund S. Purification and characterization of a manganese containing superoxide dismutase from bovine heart mitochondria. Int J Biochem. 1978;9(5):299–306. doi: 10.1016/0020-711x(78)90101-5. [DOI] [PubMed] [Google Scholar]
  14. Marklund S. Spectrophotometric study of spontaneous disproportionation of superoxide anion radical and sensitive direct assay for superoxide dismutase. J Biol Chem. 1976 Dec 10;251(23):7504–7507. [PubMed] [Google Scholar]
  15. McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
  16. Misra H. P., Fridovich I. Inhibition of superoxide dismutases by azide. Arch Biochem Biophys. 1978 Aug;189(2):317–322. doi: 10.1016/0003-9861(78)90218-7. [DOI] [PubMed] [Google Scholar]
  17. Rigo A., Viglino P., Rotilio G. Polarographic determination of superoxide dismutase. Anal Biochem. 1975 Sep;68(1):1–8. doi: 10.1016/0003-2697(75)90672-7. [DOI] [PubMed] [Google Scholar]
  18. Salin M. L., Day E. D., Jr, Crapo J. D. Isolation and characterization of a manganese-containing superoxide dismutase from rat liver. Arch Biochem Biophys. 1978 Apr 15;187(1):223–228. doi: 10.1016/0003-9861(78)90027-9. [DOI] [PubMed] [Google Scholar]
  19. Weisiger R. A., Fridovich I. Mitochondrial superoxide simutase. Site of synthesis and intramitochondrial localization. J Biol Chem. 1973 Jul 10;248(13):4793–4796. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES