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. 1975 Sep;72(9):3711–3715. doi: 10.1073/pnas.72.9.3711

Antigenic and enzymatic architecture of Micrococcus lysodeikticus membranes established by crossed immunoelectrophoresis.

P Owen, M R Salton
PMCID: PMC433067  PMID: 127177

Abstract

By crossed immunoelectrophoresis with membrane antiserum, 17 antigens have been detected in fractions from plasma membranes of M. lysodeikticus solubilized with Triton X-100. Absorption tests with protoplasts have demonstrated that eight of the antigens are expressed on the surface. Of these antigens the major one has been identified as a succinylated mannan. Five of the principal immunoprecipitates unaffected by absorption with protoplasts were shown by zymograms to possess the following enzymic activites: succinate dehydrogenase (EC 1.3.99.1), ATPase (EC 3.6.1.3), NADH dehyrogenase (EC 1.6.99.3)(two separate components), and malate dehydrogenase (EC 1.1.1.37). These enzymes or enzyme-complexes are, therefore, not expressed on the outer surface of the protoplast membrane.

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Selected References

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

  1. Blomberg F., Raftell M. Enzyme polymorphism in rat-liver microsomes and plasma membranes. 1. An immunochemical study of multienzyme complexes and other enzyme-active antigens. Eur J Biochem. 1974 Nov 1;49(1):21–29. doi: 10.1111/j.1432-1033.1974.tb03807.x. [DOI] [PubMed] [Google Scholar]
  2. Bog-Hansen T. C. Crossed immuno-affinoelectrophoresis. An analytical method to predict the result of affinity chromatography. Anal Biochem. 1973 Dec;56(2):480–488. doi: 10.1016/0003-2697(73)90215-7. [DOI] [PubMed] [Google Scholar]
  3. Doyle R. J., Woodside E. E., Fishel C. W. Protein-polyelectrolyte interactions. The concanavalin A precipitin reaction with polyelectrolytes and polysaccharide derivatives. Biochem J. 1968 Jan;106(1):35–40. doi: 10.1042/bj1060035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fukui Y., Nachbar M. S., Salton M. R. Immunological properties of Micrococcus lysodeikticus membranes. J Bacteriol. 1971 Jan;105(1):86–92. doi: 10.1128/jb.105.1.86-92.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ghosh B. K. The mesosome--a clue to the evolution of the plasma membrane. Subcell Biochem. 1974 Dec;3(4):311–367. [PubMed] [Google Scholar]
  6. Harboe N., Ingild A. Immunization, isolation of immunoglobulins, estimation of antibody titre. Scand J Immunol Suppl. 1973;1:161–164. doi: 10.1111/j.1365-3083.1973.tb03798.x. [DOI] [PubMed] [Google Scholar]
  7. Johansson K. E., Hjertén S. Localization of the Tween 20-soluble membrane proteins of Acholeplasma laidlawii by crossed immunoelectrophoresis. J Mol Biol. 1974 Jun 25;86(2):341–348. doi: 10.1016/0022-2836(74)90023-0. [DOI] [PubMed] [Google Scholar]
  8. LAURELL C. B. ANTIGEN-ANTIBODY CROSSED ELECTROPHORESIS. Anal Biochem. 1965 Feb;10:358–361. doi: 10.1016/0003-2697(65)90278-2. [DOI] [PubMed] [Google Scholar]
  9. Oppenheim J. D., Salton M. R. Localization and distribution of Micrococcus lysodeikticus membrane ATPase determined by ferritin labeling. Biochim Biophys Acta. 1973 Mar 16;298(2):297–322. doi: 10.1016/0005-2736(73)90360-x. [DOI] [PubMed] [Google Scholar]
  10. Owen P., Freer J. H. Isolation and properties of mesosomal membrane fractions from Micrococcus lysodeikticus. Biochem J. 1972 Oct;129(4):907–917. doi: 10.1042/bj1290907. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Owen P., Salton M. R. A succinylated mannan in the membrane system of Micrococcus lysodeikticus. Biochem Biophys Res Commun. 1975 Apr 21;63(4):875–880. doi: 10.1016/0006-291x(75)90649-x. [DOI] [PubMed] [Google Scholar]
  12. Raftell M., Blomberg F. Enzyme polymorphism in rat-liver microsomes and plasma membranes. 2. An immunochemical comparison of enzyme-active antigens solubilized by detergents, papain or phospholipases. Eur J Biochem. 1974 Nov 1;49(1):31–39. doi: 10.1111/j.1432-1033.1974.tb03808.x. [DOI] [PubMed] [Google Scholar]
  13. Reusch V. M., Jr, Burger M. M. The bacterial mesosome. Biochim Biophys Acta. 1973 Apr 3;300(1):79–104. doi: 10.1016/0304-4157(73)90012-9. [DOI] [PubMed] [Google Scholar]
  14. Salton M. R. Bacterial membranes. CRC Crit Rev Microbiol. 1971 May;1(1):161–197. doi: 10.3109/10408417109104480. [DOI] [PubMed] [Google Scholar]
  15. Salton M. R., Schor M. T. Subunit structure and properties of two forms of adenosine triphosphatase released from Micrococcus lysodeikticus membranes. Biochem Biophys Res Commun. 1972 Oct 17;49(2):350–357. doi: 10.1016/0006-291x(72)90417-2. [DOI] [PubMed] [Google Scholar]
  16. So L. L., Goldstein I. J. Protein-carbohydrate interaction. IX. Application of the quantitative hapten inhibition technique to polysaccharide-concanavalin A interaction. Some comments on the forces involved n concanavalin A-polysaccharide interaction. J Immunol. 1967 Jul;99(1):158–163. [PubMed] [Google Scholar]
  17. Weeke B. A manual of quantitative immunoelectrophoresis. Methods and applications. 1. General remarks on principles, equipment, reagents and procedures. Scand J Immunol Suppl. 1973;1:15–35. doi: 10.1111/j.1365-3083.1973.tb03776.x. [DOI] [PubMed] [Google Scholar]

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