Loss of tryptophan associated with photo polymerization and yellowing of proteins exposed to light over 300 nm

26Citations
Citations of this article
6Readers
Mendeley users who have this article in their library.

Abstract

S Carboxymethyl lysozyme and S carboxymethyl ribonuclease A were irradiated with light of wavelength greater than 300nm. Photo oxidative loss of tryptophan from the S carboxymethyl lysozyme was accompanied by yellowing of the protein and the formation of covalently cross linked polymers. S carboxymethyl ribonuclease, which contains no tryptophan, showed little yellowing and no polymer formation. The irradiated S carboxymethyl lysozyme was similar to the proteins of the brown cataractous human lens nucleus and to bovine lens proteins exposed to sunlight in vitro in that it was insoluble in non denaturing solvents, contained a new fluorescence, was brown in color, and contained covalent cross links that are not disulphide bonds.

Cite

CITATION STYLE

APA

Dilley, K. J. (1973). Loss of tryptophan associated with photo polymerization and yellowing of proteins exposed to light over 300 nm. Biochemical Journal, 133(4), 821–826. https://doi.org/10.1042/bj1330821

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free