Literature DB >> 6154045

Acetate kinase in the genus Veillonella: effect of succinate, serological cross-reactivity, and separation by electrophoresis.

F Yoshimura, N Kasai, B Sugawara, T Suzuki.   

Abstract

Acetate kinases from the genus Veillonella were divided into two types: a succinate-stimulated enzyme and a succinate-independent enzyme. Three strains, V. parvula ATCC 17743 (antigenic group II), V. parvula ATCC 17744 (V), and V. parvula ATCC 10790 (VI), contained the succinate-stimulated enzyme. Among four types strains of V. alcalescens, three strains, ATCC 17747 (I), ATCC 17746 (III), and ATCC 17748 (VII), contained the succinate-independent enzyme, whereas only one strain, ATCC 17745 (IV), contained the succinate-stimulated enzyme. Small amounts of antiserum to the purified acetate kinase from V. alcalescens ATCC 17748 completely inhibited the purified and crude enzyme activity from the strain. Classification of the enzymes on the basis of stimulation by succinate was consistent with classification based on serological reactions using the antiserum as an independent parameter. The succinate-stimulated enzyme could be separated into two classes according to the degree of sensitivity to succinate: (i) enzymes from V. parvula ATCC 17744 and V. alcalescens ATCC 17745, which could be demonstrated on gel after electrophoresis by a histochemical method to be highly stimulated by the presence of succinate in the reaction mixture, and (ii) enzymes from V. parvula ATCC 10790 and V. parvula ATCC 17743, which could be easily demonstrated without succinate. Four groups of acetate kinases from the genus Veillonella were separated by gel electrophoretic mobility. The results showed that almost all enzymes from the seven type strains were heterogeneous at the molecular level.

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Year:  1980        PMID: 6154045      PMCID: PMC293829          DOI: 10.1128/jb.141.3.1312-1319.1980

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  18 in total

1.  DISC ELECTROPHORESIS IN POLYACRYLAMIDE GELS: EXTENSION TO NEW CONDITIONS OF PH AND BUFFER.

Authors:  D E WILLIAMS; R A REISFELD
Journal:  Ann N Y Acad Sci       Date:  1964-12-28       Impact factor: 5.691

2.  Acetate kinase from Veillonella alcalescens. Regulation by succinate and substrates.

Authors:  M J Griffith; J S Nishimura
Journal:  J Biol Chem       Date:  1979-07-25       Impact factor: 5.157

3.  Acetate kinase from Veillonella alcalescens. Purification and physical properties.

Authors:  M J Griffith; J S Nishimura
Journal:  J Biol Chem       Date:  1979-01-25       Impact factor: 5.157

4.  Purification of acetate kinase by affinity chromatography.

Authors:  J R Swartz; G W Pace; B A Solomon; C K Colton; M C Archer
Journal:  Prep Biochem       Date:  1978

5.  Purification and characterization of acetate kinase from veillonella alcalescens ATCC 17748.

Authors:  F Yoshimura
Journal:  Arch Biochem Biophys       Date:  1978-08       Impact factor: 4.013

6.  Membrane-bound adenosine triphosphatase of Escherichia coli. I. Partial purification and properties.

Authors:  H Kobayashi; Y Anraku
Journal:  J Biochem       Date:  1972-03       Impact factor: 3.387

7.  The Genus Veillonella IV. Serological Groupings, and Genus and Species Emendations.

Authors:  M Rogosa
Journal:  J Bacteriol       Date:  1965-09       Impact factor: 3.490

8.  Acetate kinase from Veillonella alcalescens. Regulation of enzyme activity by succinate and substrates.

Authors:  C M Bowman; R O Valdez; J S Nishimura
Journal:  J Biol Chem       Date:  1976-05-25       Impact factor: 5.157

9.  Purification of acetokinase from Desulfovibrio desulfuricans.

Authors:  M S Brown; J M Akagi
Journal:  J Bacteriol       Date:  1966-10       Impact factor: 3.490

10.  ULTRASTRUCTURE OF VEILLONELLA AND MORPHOLOGICAL CORRELATION OF AN OUTER MEMBRANE WITH PARTICLES ASSOCIATED WITH ENDOTOXIC ACTIVITY.

Authors:  H A BLADEN; S E MERGENHAGEN
Journal:  J Bacteriol       Date:  1964-11       Impact factor: 3.490

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