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Studies on Mg- (Ca-)activated Adenosine Triphosphatase from 46, Page 1 of 1

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/content/journal/micro/10.1099/00221287-105-2-343
1978-04-01
2021-07-23
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References

  1. Abrams A. 1965; The release of bound adenosine triphosphatase from isolated bacterial membranes and the properties of the solubilized enzyme. Journal of Biological Chemistry 240:3675–3681
    [Google Scholar]
  2. Abrams A., Smith J. B. 1974; Bacterial membrane ATPase. In The Enzymes 10 pp. 395–429 Boyer P. D. Edited by New York:: Academic Press.;
    [Google Scholar]
  3. Abrams A., McNamara P., Johnson F. B. 1960; Adenosine triphosphatase in isolated bacterial membranes. Journal of Biological Chemistry 235:3659–3662
    [Google Scholar]
  4. Bonting S. L., Caravaggio L. L., Hawkins N. M. 1962; Studies on sodium-potassium- activated adenosine triphosphatase. IV. Correlation with cation transport sensitive to cardiac glycosides. Archives of Biochemistry and Biophysics 98:413–419
    [Google Scholar]
  5. Brodie A. F. 1959; Oxidative phosphorylation in fractionated bacterial systems. I. Role of soluble factors. Journal of Biological Chemistry 234:398–404
    [Google Scholar]
  6. Evans D. J.Jr 1969; Membrane adenosine triphosphatase of Escherichia coli: activation by calcium ions and inhibition by monovalent cations. Journal of Bacteriology 100:914–922
    [Google Scholar]
  7. Evans D. J.Jr 1970; Membrane Mg2+- (Ca2+)-activated adenosine triphosphatase of Escherichia coli: characterization in the membrane-bound and solubilized states. Journal of Bacteriology 104:1203–1212
    [Google Scholar]
  8. Fiske C. H., SubbaRow Y. 1925; The colorimetric determination of phosphorus. Journal of Biological Chemistry 66:375–400
    [Google Scholar]
  9. Greenawalt J. W., Weibull C., Low H. 1962; The hydrolysis of adenosine triphosphate by cell fractions of Bacillus megaterium. II. Stimulation and inhibition of the enzyme activities. Journal of Biological Chemistry 237:853–858
    [Google Scholar]
  10. Harold F. M., Baarda J. R. 1968; Effects of nigericin and monactin on cation permeability of Streptococcus faecalis and metabolic capacities of potassium-depleted cells. Journal of Bacteriology 95:816–823
    [Google Scholar]
  11. Hayashi M., Uchida R. 1965; A cation activated adenosine triphosphatase in cell membranes of halophilic Vibrio parahaemolyticus.. Biochimica et biophysica acta 110:207–209
    [Google Scholar]
  12. Higashi T., Kalra V. K., Lee S.-H., Bogin E., Brodie A. F. 1975; Energy-transducing membrane-bound coupling factor ATPase from Mycobacterium phlei. I. Purification, homogeneity and properties. Journal of Biological Chemistry 250:6541–6548
    [Google Scholar]
  13. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  14. Youmans G. P., Karlson A. G. 1947; Streptomycin sensitivity of tubercle bacilli. Studies on recently isolated tubercle bacilli and the development of resistance to streptomycin in vivo.. American Review of Tuberculosis 55:529–535
    [Google Scholar]
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