Absorption Spectrum of Rhodopsin denatured with Acid View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1968-06

AUTHORS

YUJI KITO, TATSUO SUZUKI, AMI AZUMA, YUZO SEKOGUTI

ABSTRACT

THE visual pigment rhodopsin is composed of the chromophore, retinal, and the protein moiety, opsin1,2. Retinal and opsin are considered to be bound to each other primarily by a Schiff base linkage, and secondarily by a stereospecific link3–5. An ε-amino group, probably of a lysine residue in opsin, may participate with the Schiff base binding6,7. The nature of the secondary link is still obscure, but its existence is suggested by: (1) rhodopsin can be regenerated from opsin and 11-cis retinal beyond other isomers1,2; (2) a bathochromic shift of absorption spectrum of retinal in rhodopsin cannot be simply explained by the Schiff base with amino compounds8; (3) Schiff base linkages are usually unstable at pHs at which rhodopsin is stable8,9; (4) when rhodopsin is attacked by denaturants of protein or by heat, bleaching results10,11,16; (5) retinal in rhodopsin has been found to be fixed asymmetrically on the protein12–15. More... »

PAGES

955

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/218955a0

DOI

http://dx.doi.org/10.1038/218955a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1004963066

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/5681237


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