Lipid to Protein Chromophore Transfer in the Photolysis of Visual Pigments View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1969-01

AUTHORS

R. P. POINCELOT, P. G. MILLAR, R. L. KIEL jun., E. W. ABRAHAON

ABSTRACT

VERTEBRATE visual pigments in their native state are the principal components of the membranes of rod and cone outer distal segments1. Like all membrane structures they have a predominantly lipoprotein composition2,3. The traditional picture of the native form of these pigments, developed largely from their preponderant protein properties4, is one of a polyene chromophore bound to a protein through a Schiff base linkage5 and, indeed, the recent demonstration of Bownds6 and Aktar7 of the NaBH4 reductive affixation of the retinylidene chromophore to the ε-amino group of a lysine residue in irradiated bovine rhodopsin seems to support this notion. But to assume that this is the binding site in native rhodopsin discounts the possibility of migration of the chromophore in the early stages of the physiological process, and further implies that the chromophore could not have migrated to this particular ε-amino group of lysine from some other site in the near neutral pH conditions of the NaBH4 reduction6,7 where Schiff bases are known to hydrolyse readily and undergo inline exchange8. More... »

PAGES

256-257

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/221256a0

DOI

http://dx.doi.org/10.1038/221256a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022794208

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/5763079


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