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PMID: 13346045 Published · ppublish English Journal Article

The stability of rhodopsin and opsin; effects of pH and aging.

The Journal of general physiology ·Vol. 39 ·No. 6 ·1956-07-20 ·Pages 923-33

RADDING CM, WALD G

Abstract

THE STABILITY OF CATTLE RHODOPSIN AND OF ITS PROTEIN MOIETY OPSIN TOWARD ACIDS AND ALKALIES AND ON AGING WAS DETERMINED BY TWO CRITERIA: maintenance of absorption spectrum, and capacity to regenerate after exposure to light. On storage at 3 degrees C. at pH near neutrality, the absorption spectrum in the visible region may remain unchanged for as long as 6 months; but the regenerability progressively declines, at very different rates in different preparations. The cause of this decline has not been determined. It may involve denaturation at sites other than the retinene-protein bond, which by the evidence of the absorption spectrum remains intact. Cattle rhodopsin maintains its absorption spectrum at any pH from 3.9-9.6 for at least an hour at 25-27 degrees C. To both sides of this pH range the pigment bleaches, the extinction falling to half in 1 hour at pH 3.3 and 10.5. The exposure of rhodopsin to light greatly increases the vulnerability of the product (opsin) to acids and bases. Opsin rapidly loses its capacity to regenerate rhodopsin to both sides of the range of pH 5.5-7.0. Half the regenerability is lost within 45 seconds at pH 3.4 and 9.1; and within 1 hour at pH 5 and 8.

Keywords
HYDROGEN-ION CONCENTRATION/effects RHODOPSIN/physiology
MeSH Terms
Animals Cattle Hydrogen-Ion Concentration Light Opsins Retinaldehyde Rhodopsin/physiology Rod Opsins
Chemicals
Opsins Rod Opsins Rhodopsin Retinaldehyde
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
RADDING C M
WALD G
References (6)
6 references, click to expand
  1. Cis-trans isomers of vitamin A and retinene in the rhodopsin system.
    J Gen Physiol. 1952 Nov;36(2):269-315 PMID: 13011282
  2. The molar extinction of rhodopsin.
    J Gen Physiol. 1953 Nov 20;37(2):189-200 PMID: 13109155
  3. Acid-base properties of rhodopsin and opsin.
    J Gen Physiol. 1956 Jul 20;39(6):909-22 PMID: 13346044
  4. Iodopsin.
    J Gen Physiol. 1955 May 20;38(5):623-81 PMID: 14367777
  5. The role of sulfhydryl groups in the bleaching and synthesis of rhodopsin.
    J Gen Physiol. 1952 May;35(5):797-821 PMID: 14955620
  6. The light reaction in the bleaching of rhodopsin.
    Science. 1950 Feb 17;111(2877):179-81 PMID: 15403120
Article Info
Journal
The Journal of general physiology
Abbr.
J Gen Physiol
ISSN
0022-1295
Published
1956-07-20
Pages
923-33
Language
English
Region
United States
NLM ID
2985110R
PMCID
PMC2147573
Subset
OM
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