PMID: 2493816Mar 16, 1989Paper

Immunological comparison of subunits isolated from various hydrogenases of aerobic hydrogen bacteria

Biochimica Et Biophysica Acta
B LorenzH G Schlegel

Abstract

Polyclonal, monospecific antibodies were produced against the two subunits (Mr 62,000, and Mr 31,000), isolated from the membrane-bound hydrogenase of Alcaligenes eutrophus H16. The antibodies (IgG fractions) were purified from crude sera by Protein A-Sepharose CL-4B chromatography. By double immunodiffusion assays and tandem-crossed immunoelectrophoresis the large and the small subunit were demonstrated not to be immunologically related. Immunological comparison of these subunits with the four non-identical subunits (Mr 63,000, 56,000, 30,000 and 26,000) of the NAD-linked, soluble hydrogenase from A. eutrophus H16 showed that the subunits of the membrane-bound hydrogenase did not cross-react with any of the antibodies raised against the four subunits of the NAD-linked enzyme and that, vice versa, none of these four subunits cross-reacted with antibodies raised against the two subunits of the membrane-bound hydrogenase. This means that A. eutrophus H16 contains altogether six non-identical immunologically unrelated hydrogenase polypeptides. The membrane-bound hydrogenases were isolated and purified from various aerobic H2-oxidizing bacteria: A. eutrophus H16, A. eutrophus type strain, A. eutrophus CH34, A. eutrophus Z1, A. hydr...Continue Reading

References

Oct 1, 1979·Analytical Biochemistry·G J Dimitriadis
Dec 16, 1987·Biochemical and Biophysical Research Communications·B C PrickrilJ LeGall
Dec 1, 1987·Molecular & General Genetics : MGG·A BirkmannA Böck
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Oct 1, 1983·Analytical Biochemistry·F G Plumley, G W Schmidt

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Citations

Dec 1, 1990·FEMS Microbiology Reviews·J N Reeve, G S Beckler
Oct 1, 1992·Journal of Bacteriology·C KortlükeB Friedrich
Oct 1, 1992·Journal of Bacteriology·C Kortlüke, B Friedrich
Dec 30, 1994·Biochimica Et Biophysica Acta·S P Albracht
Jun 1, 1992·Analytical Biochemistry·D M Ferber, R J Maier

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