1887

Abstract

Summary: Crystalline neuraminidase prepared from culture fluids by Ada, French & Lind (1961) was examined by moving boundary electrophoresis, analytical ultracentrifugation and diffusion. The various corresponding physical constants were obtained. The results indicated that, within the limits of the methods used, the crystalline protein was enzyme and was homogeneous.

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/content/journal/micro/10.1099/00221287-24-3-423
1961-03-01
2024-04-25
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References

  1. Ada G. L., French E. L., Lind P. E. 1961; Purification and properties of neuraminidase from Vibrio cholerae . J. gen. Microbiol 24:409
    [Google Scholar]
  2. French E. L., Ada G. L. 1959; Stimulation of the production of neuraminidase in Vibrio cholerae cultures by N-acetylneuraminic acid and sialyl lactose. J. gen. Microbiol 21:550
    [Google Scholar]
  3. Moore D. H., Opperman K. 1956; Adaptation of combined interferometric and phase-plate gradient optics to electrophoresis. Biochim. biophys. Acta 22:136
    [Google Scholar]
  4. Schramm G., Mohr E. 1959; Purification of neuraminidase from Vibrio cholerae . Nature; Lond: 1831677
    [Google Scholar]
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