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:

Effect of Polylysine on the Absorption Spectrum of Hæmin

Abstract

THIS is a preliminary report on a ‘polybase effect’ consisting of a considerable change in the spectrum of hæmin on its interaction with polylysine in alkaline solution. Two different types of complex are formed with poly-L-lysine which may be associated with the folded and unfolded structure of the peptide. These simple hæmin–polypeptide complexes are considered to serve as models for iron–porphyrin-containing enzymes, and it is hoped that they will add to our knowledge of the prosthetic group-protein interaction and of the catalytic properties connected with it.

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. Applequist, J., and Doty, P., Abstr. Amer. Chem. Soc., 133rd Meeting, San Francisco, 32, Q (1958). Applequist, J. B., Ph.D. thesis, Harvard University (April 1959).

  2. Ehrenberg, A., and Theorell, H., Acta Chem. Scand., 9, 1193 (1955).

    Article  CAS  Google Scholar 

  3. Arndt, U. W., and Riley, D. P., Phil. Trans. Roy. Soc., A, 247, 409 (1955).

    Article  ADS  Google Scholar 

  4. Lemberg, R., and Legge, J. W., “Hematin Compounds and Bile Pigments” (Interscience, New York–London, 1949).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

BLAUER, G. Effect of Polylysine on the Absorption Spectrum of Hæmin. Nature 189, 396–397 (1961). https://doi.org/10.1038/189396a0

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/189396a0

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