Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Dissociation of Ovalbumin in Urea Solvent

Abstract

THE physical molecule in solution is that unit which will acquire from thermal vibrations an average of 1/2 kT ergs of energy for each of three translational degrees of freedom. It is becoming increasingly evident that the weights of protein molecules defined in this way may change with solvent temperature, dielectric constant, protein or salt concentration, and other factors. Numerous studies from this Laboratory have demonstrated the effect of change of pH of the solvent medium in the dissociation and association of the molecules comprising the fundamental component.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Watson, Arrhenius and Williams, NATURE, 137, 322 (1936).

    Article  ADS  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

WILLIAMS, J., WATSON, C. Dissociation of Ovalbumin in Urea Solvent. Nature 139, 506–507 (1937). https://doi.org/10.1038/139506a0

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/139506a0

This article is cited by

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing