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. 1973 Feb;113(2):937–945. doi: 10.1128/jb.113.2.937-945.1973

Physiological Studies of Methane- and Methanol-Oxidizing Bacteria: Immunological Comparison of a Primary Alcohol Dehydrogenase from Methylococcus capsulatus and Pseudomonas sp. M27

R N Patel a,1, W J Mandy a, D S Hoare a,2
PMCID: PMC285312  PMID: 4120569

Abstract

A primary alcohol dehydrogenase was purified from cell extracts of two apparently unrelated microorganisms, namely, Pseudomonas sp. M27 and Methylococcus capsulatus. Rabbit antiserum prepared against the purified enzyme from M. capsulatus revealed distinctive antigenic determinants by quantitative and gel precipitin reactions. Rabbit antiserum to M27 enzyme detected both distinctive and shared antigenic determinants. Certain methane- and methanol-oxidizing bacteria were grouped on the basis of serological cross-reacting enzyme specificities.

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Selected References

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

  1. Anthony C., Zatman L. J. The microbial oxidation of methanol. 1. Isolation and properties of Pseudomonas sp. M27. Biochem J. 1964 Sep;92(3):609–614. doi: 10.1042/bj0920609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anthony C., Zatman L. J. The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27. Biochem J. 1967 Sep;104(3):953–959. doi: 10.1042/bj1040953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Anthony C., Zatman L. J. The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group. Biochem J. 1967 Sep;104(3):960–969. doi: 10.1042/bj1040960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. CONTI S. F., HIRSCH P. BIOLOGY OF BUDDING BACTERIA. 3. FINE STRUCTURE OF RHODOMICROBIUM AND HYPHOMICROBIUM SPP. J Bacteriol. 1965 Feb;89:503–512. doi: 10.1128/jb.89.2.503-512.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dahl J. S., Mehta R. J., Hoare D. S. New obligate methylotroph. J Bacteriol. 1972 Feb;109(2):916–921. doi: 10.1128/jb.109.2.916-921.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Davies S. L., Whittenbury R. Fine structure of methane and other hydrocarbon-utilizing bacteria. J Gen Microbiol. 1970 May;61(2):227–232. doi: 10.1099/00221287-61-2-227. [DOI] [PubMed] [Google Scholar]
  7. Foster J. W., Davis R. H. A methane-dependent coccus, with notes on classification and nomenclature of obligate, methane-utilizing bacteria. J Bacteriol. 1966 May;91(5):1924–1931. doi: 10.1128/jb.91.5.1924-1931.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HIRSCH P., CONTI S. F. BIOLOGY OF BUDDING BACTERIA. I. ENRICHMENT, ISOLATION AND MORPHOLOGY OF HYPHOMICROBIUM SPP. Arch Mikrobiol. 1964 Jun 26;48:339–357. doi: 10.1007/BF00405978. [DOI] [PubMed] [Google Scholar]
  9. Kekwick R. A. The serum proteins in multiple myelomatosis. Biochem J. 1940 Sep;34(8-9):1248–1257. doi: 10.1042/bj0341248. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LEVY H. B., SOBER H. A. A simple chromatographic method for preparation of gamma globulin. Proc Soc Exp Biol Med. 1960 Jan;103:250–252. doi: 10.3181/00379727-103-25476. [DOI] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. London J., Meyer E. Y., Kulczyk S. Comparative biochemical and immunological study of malic enzyme from two species of lactic acid bacteria: evolutionary implications. J Bacteriol. 1971 Apr;106(1):126–137. doi: 10.1128/jb.106.1.126-137.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Murphy T. M., Mills S. E. Immunochemical and enzymatic comparisons of the tryptophan synthase alpha subunits from five species of Enterobacteriaceae. J Bacteriol. 1969 Mar;97(3):1310–1320. doi: 10.1128/jb.97.3.1310-1320.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Patel R. N., Hoare D. S. Physiological studies of methane and methanol-oxidizing bacteria: oxidation of C-1 compounds by Methylococcus capsulatus. J Bacteriol. 1971 Jul;107(1):187–192. doi: 10.1128/jb.107.1.187-192.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. SCHEIDEGGER J. J. Une micro-méthode de l'immuno-electrophorèse. Int Arch Allergy Appl Immunol. 1955;7(2):103–110. [PubMed] [Google Scholar]
  16. Stanier R. Y., Wachter D., Gasser C., Wilson A. C. Comparative immunological studies of two Pseudomonas enzymes. J Bacteriol. 1970 May;102(2):351–362. doi: 10.1128/jb.102.2.351-362.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Whittenbury R., Davies S. L., Davey J. F. Exospores and cysts formed by methane-utilizing bacteria. J Gen Microbiol. 1970 May;61(2):219–226. doi: 10.1099/00221287-61-2-219. [DOI] [PubMed] [Google Scholar]
  18. Whittenbury R., Phillips K. C., Wilkinson J. F. Enrichment, isolation and some properties of methane-utilizing bacteria. J Gen Microbiol. 1970 May;61(2):205–218. doi: 10.1099/00221287-61-2-205. [DOI] [PubMed] [Google Scholar]

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