Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1987 Apr;169(4):1651–1655. doi: 10.1128/jb.169.4.1651-1655.1987

Purification and characterization of ribitol-5-phosphate and xylitol-5-phosphate dehydrogenases from strains of Lactobacillus casei.

S Z Hausman, J London
PMCID: PMC211995  PMID: 3104310

Abstract

A simple three-step procedure is described which yields electrophoretically homogeneous preparations of ribitol-5-phosphate dehydrogenase and xylitol-5-phosphate dehydrogenase. The former enzyme is a 115,000-molecular-weight protein composed of two subunits of identical size and is specific for its substrate, ribitol. The xylitol-5-phosphate dehydrogenase exists as a tetrameric protein with a molecular weight of 180,000; this enzyme oxidizes the phosphate esters of both xylitol and D-arabitol. Characterization of the physical, kinetic, and immunological properties of the two enzymes suggests that the functionally similar enzymes may not be structurally related.

Full text

PDF
1651

Images in this article

1653Image
on p.1653
1653Image
on p.1653
1654Image
on p.1654
1654Image
on p.1654

Selected References

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

  1. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Batteiger B., Newhall W. J., 5th, Jones R. B. The use of Tween 20 as a blocking agent in the immunological detection of proteins transferred to nitrocellulose membranes. J Immunol Methods. 1982 Dec 30;55(3):297–307. doi: 10.1016/0022-1759(82)90089-8. [DOI] [PubMed] [Google Scholar]
  3. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  4. Doten R. C., Mortlock R. P. Characterization of xylitol-utilizing mutants of Erwinia uredovora. J Bacteriol. 1985 Feb;161(2):529–533. doi: 10.1128/jb.161.2.529-533.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. EFTHYMIOU C., HANSEN P. A. An antigenic analysis of Lactobacillus acidophilus. J Infect Dis. 1962 May-Jun;110:258–267. doi: 10.1093/infdis/110.3.258. [DOI] [PubMed] [Google Scholar]
  6. London J., Chace N. M. New pathway for the metabolism of pentitols. Proc Natl Acad Sci U S A. 1977 Oct;74(10):4296–4300. doi: 10.1073/pnas.74.10.4296. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. London J., Chace N. M. Pentitol metabolism in Lactobacillus casei. J Bacteriol. 1979 Dec;140(3):949–954. doi: 10.1128/jb.140.3.949-954.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. London J., Hausman S. Z. Purification and characterization of the IIIXtl phospho-carrier protein of the phosphoenolpyruvate-dependent xylitol:phosphotransferase found in Lactobacillus casei C183. J Bacteriol. 1983 Nov;156(2):611–619. doi: 10.1128/jb.156.2.611-619.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. London J., Hausman S. Xylitol-mediated transient inhibition of ribitol utilization by Lactobacillus casei. J Bacteriol. 1982 May;150(2):657–661. doi: 10.1128/jb.150.2.657-661.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. London J., Kline K. Aldolase of lactic acid bacteria: a case history in the use of an enzyme as an evolutionary marker. Bacteriol Rev. 1973 Dec;37(4):453–478. doi: 10.1128/br.37.4.453-478.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. London J., Meyer E. Y., Kulczyk S. R. Detection of relationships between Streptococcus faecalis and Lactobacillus casei by immunological studies with two forms of malic enzyme. J Bacteriol. 1971 Oct;108(1):196–201. doi: 10.1128/jb.108.1.196-201.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Meun D. H., Smith K. C. A micro phosphate method. Anal Biochem. 1968 Dec;26(3):364–368. doi: 10.1016/0003-2697(68)90197-8. [DOI] [PubMed] [Google Scholar]
  13. Nowlan S. S., Deibel R. H. Group Q streptococci. I. Ecology, serology, physiology, and relationship to established enterococci. J Bacteriol. 1967 Aug;94(2):291–296. doi: 10.1128/jb.94.2.291-296.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES