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Archives of Microbiology

, Volume 155, Issue 1, pp 28–34 | Cite as

An immunological study of corrinoid proteins from bacteria revealed homologous antigenic determinants of a soluble corrinoid-dependent methyltransferase and corrinoid-containing membrane proteins from Methanobacterium species

  • Erhard Stupperich
  • Andreas Juza
  • Christoph Eckerskorn
  • Lillian Edelmann
Original Papers

Abstract

The hypothesis of common epitopes in corrinoid-dependent enzymes was tested by a monospecific polyclonal antiserum against the 33 kDa corrinoid-containing membrane protein from Methanobacterium thermoautotrophicum Marburg. Cross-reaction was detected with the 33 kDa and the 31 kDa subunits of the corrinoid-containing enriched 5-methyl-H4MPT: 5-hydroxybenzimidazolyl cobamide methyltransferase from the cytoplasmic fraction and a 33 kDa protein from the membrane fraction of Methanobacterium thermoauto-trophicum ΔH. This indicates that both proteins have similar antigenic determinants and that they may have similar function as methyltransfer proteins. Also a soluble 20 kDa protein of yet unknown function from Clostridium barkeri cross-reacted with the antiserum. No cross-reactions were observed with the purified corrinoid-containing 2-methyleneglutarate mutase from C. barkeri, the corrinoid/iron-sulfur protein from C. thermoaceticum, the carbon monoxide dehydrogenases from C. thermoaceticum and Methanothrix soehngenii, and the corrinoid-binding protein intrinsic factor from porcine gastric mucosa. Also cell extracts from the corrinoid-rich bacteria Sporomusa ovata, Methanolobus tindarius, Chloroflexus aurantiacus, Propionibacterium shermanii, the membrane fraction and the cytoplasmic fraction of Methanococcus voltae or extracts from human liver, contained no antibody combining sites others than with the preimmunological serum. These findings indicate, that many corrinoid-containing proteins from bacteria have no common antigenic determinants.

Key words

Methylmalonyl-CoA mutase 2-Methyleneglutarate mutase Carbon monoxide dehydrogenase Adenosylcobalamin Methyl-vitamin B12 Methanobacterium thermoautotrophicum Propionibacterium shermanii 

Abbreviations

CH3-H4MPT

N5-methyl-tetrahydromethanopterin

SDS-PAGE

sodium dodecyl sulfate polyacrylamide gel electrophoresis

ELISA

enzyme linked immunosorbent assay

DSM

Deutsche Sammlung von Mikroorganismen

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Copyright information

© Springer-Verlag 1990

Authors and Affiliations

  • Erhard Stupperich
    • 1
  • Andreas Juza
    • 1
  • Christoph Eckerskorn
    • 2
  • Lillian Edelmann
    • 3
  1. 1.Abteilung Angewandte MikrobiologieUniversität UlmUlmFederal Republic of Germany
  2. 2.Max Planck Institut für biochemie-GenzentrumMartinsriedFederal Republic of Germany
  3. 3.Lehrstuhl für BiochemieInstitut für Organische Chemie der Universität KarlsruheKarlsruheFederal Republic of Germany

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