Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 31 January 1958:
Vol. 127. no. 3292, pp. 222 - 249
DOI: 10.1126/science.127.3292.222
Prev | Table of Contents | Next

Articles

Human Rhodopsin

George Wald 1 and Paul K. Brown 1

1 Members of the staff of the Biological Laboratories, Harvard University, Cambridge, Mass.

Human rhodopsin in aqueous solution has lgrmax. of 493 mµ and is lower in the spectrum than the rhodopsins of all other known vertebrates, with the exception of certain deep-sea fishes. Its molar extinction is 40,000 ± 800. Like other rhodopsins, it bleaches to a mixture of opsin and all-trans retinene and is resynthesized by incubating opsin with neo-b (11-cis) retinene. The regenerated rhodopsin has the same lgrmax. as the extracted pigment; this is due, therefore, not to an unusual retinene but to a characteristic human opsin. The regeneration in solution from opsin and neo-b retinene is a second-order reaction with a half-time, at 29.5° C, of about 2.5 minutes. This is much faster than the synthesis of rhodopsin in the living human eye, and faster than human rod dark-adaptation; the rate of both processes in vivo must be limited by reactions which precede the union of neo-b retinene with opsin, the final step in rhodopsin synthesis. In the rods, rhodopsin is virtually in the solid state—highly oriented in close relation with other highly oriented molecules. In this situation its spectrum is displaced toward the red (lgrmax 500 mµ) and is narrower than in solution. For light entering the rods axially, rhodopsin has also a considerably increased extinction, some 1.5 times higher than when randomly oriented. The spectrum of rhodopsin in rods agrees well in form and position with the spectral sensitivity of human rod vision, measured at the retinal surface.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Opsin activation of transduction in the rods of dark-reared Rpe65 knockout mice.
J. Fan, M. L Woodruff, M. C Cilluffo, R. K Crouch, and G. L Fain (2005)
J. Physiol. 568, 83-95
   Abstract »    Full Text »    PDF »
Perspectives on the counterion switch-induced photoactivation of the G protein-coupled receptor rhodopsin.
R. R. Birge and B. E. Knox (2003)
PNAS 100, 9105-9107
   Full Text »    PDF »
A Practical Method for Measuring Macular Pigment Optical Density.
B. R. Wooten, B. R. Hammond Jr., R. I. Land, and D. M. Snodderly (1999)
Invest. Ophthalmol. Vis. Sci. 40, 2481-2489
   Abstract »    Full Text »    PDF »
The Rhodopsin Content of Human Eyes.
A. B. Fulton, J. Dodge, R. M. Hansen, and T. P. Williams (1999)
Invest. Ophthalmol. Vis. Sci. 40, 1878-1883
   Abstract »    Full Text »    PDF »
Mechanisms of spectral tuning in the mouse green cone pigment.
H. Sun, J. P. Macke, and J. Nathans (1997)
PNAS 94, 8860-8865
   Abstract »    Full Text »    PDF »
Protein-Chromophore Interactions in Rhodopsin Studied by Site-directed Mutagenesis.
J. Nathans (1990)
Cold Spring Harb Symp Quant Biol 55, 621-633
   Abstract »    PDF »
Immunoreactive Opsin Content in Subretinal Fluid From Patients With Rhegmatogenous Retinal Detachments.
S. Hara, S.-i. Ishiguro, S. Hayasaka, and K. Mizuno (1987)
Arch Ophthalmol 105, 260-263
   Abstract »    PDF »
Rapid light-induced changes in near infrared transmission of rods in Bufo marinus.
H. Harary, J. Brown, and L. Pinto (1978)
Science 202, 1083-1085
   Abstract »    PDF »
Visual adaptation: effects of externally applied retinal on the light-adapted, isolated skate retina.
D. Pepperberg, M Lurie, P. Brown, and J. Dowling (1976)
Science 191, 394-396
   Abstract »    PDF »
Molecular Basis of Visual Excitation.
G. Wald (1968)
Science 162, 230-239
   PDF »
Human Color Vision and Color Blindness.
G. Wald and P. K. Brown (1965)
Cold Spring Harb Symp Quant Biol 30, 345-361
   Abstract »    PDF »
The Receptors of Human Color Vision: Action spectra of three visual pigments in human cones account for normal color vision and color-blindness.
G. Wald (1964)
Science 145, 1007-1016
   PDF »
Visual Pigments in Single Rods and Cones of the Human Retina.
P. K. Brown and G. Wald (1964)
Science 144, 45-52
   Abstract »    PDF »
Physiological Chemistry of the Eye: A Review of Papers Published During 1958.
A. M. POTTS (1959)
Arch Ophthalmol 62, 702-728
   PDF »
Optics and Visual Physiology.
A. LINKSZ (1959)
Arch Ophthalmol 61, 944-1003
   PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)