Influence of ph and urea on the ultra-violet fluorescence of several globular proteins

ABSTRACT RECENT work by Weber1–3 has shown that the ultraviolet fluorescent spectra of globular proteins differ from those predicted for the summation of the independent contributions of

their aromatic amino-acid constituents. Those examples investigated which contained tyrosine, but no tryptophan, showed a tyrosine emission spectrum, but with a reduced quantum yield. Those

containing both tyrosine and tryptophan showed an emission spectrum predominantly resembling that of tryptophan alone, with an emission maximum in the range 320–350 mµ. The present

communication will be concerned solely with proteins of the second category. Access through your institution Buy or subscribe This is a preview of subscription content, access via your

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PROTEIN Article Open access 06 November 2024 CHEMICALLY STABLE FLUORESCENT PROTEINS FOR ADVANCED MICROSCOPY Article Open access 07 November 2022 NON-FLUORESCENT TRANSIENT STATES OF TYROSINE

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Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Naval Medical Research Institute, National Naval Medical Center, R. F. STEINER * National Institute of Arthritis and

Metabolic Disease, National Institutes of Health, Bethesda, Maryland H. EDELHOCH Authors * R. F. STEINER View author publications You can also search for this author inPubMed Google Scholar

* H. EDELHOCH View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE

STEINER, R., EDELHOCH, H. Influence of _p_H and Urea on the Ultra-violet Fluorescence of Several Globular Proteins. _Nature_ 192, 873–874 (1961). https://doi.org/10.1038/192873a0 Download

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