ChemInform Abstract: Vitamin A Isomers. Part 19. (7Z)- and (7Z,9Z)-3-Dehydroretinal. Hindered Isomers of Vitamin A2 Aldehyde.

ChemInform ◽  
2010 ◽  
Vol 26 (2) ◽  
pp. no-no
Author(s):  
R. CHEN ◽  
R. S. H. LIU
Keyword(s):  
1989 ◽  
Vol 142 (1) ◽  
pp. 207-214
Author(s):  
A. T. Tsin ◽  
S. N. Gentles ◽  
E. A. Castillo

Two groups of goldfish (Carassius auratus) were subjected to light and temperature conditions known to promote a contrast in their scotopic visual pigment compositions. After 3 weeks, the porphyropsin/rhodopsin ratio in the neuroretina of these goldfish ranged from 99% porphyropsin in one group to 59% in the other. Samples of blood, liver and retinal pigment epithelium (RPE) were also removed from these animals and analysed by high-performance liquid chromatography (HPLC) for vitamin A composition. There was consistently more vitamin A2 than vitamin A1 (over 50% vitamin A2) in both vitamin A alcohol and vitamin A esters extracted from the liver and the RPE. In contrast, only 30% of all vitamin A extracted from the blood was vitamin A2. These observations suggest that it is mainly vitamin A1 that is transported in the blood, whereas vitamin A2 is selectively retained in the liver and in the RPE and used to form porphyropsin in the eye.


1952 ◽  
Vol 52 (4) ◽  
pp. 542-547 ◽  
Author(s):  
H. R. Cama ◽  
P. D. Dalvi ◽  
R. A. Morton ◽  
M. K. Salah
Keyword(s):  

1971 ◽  
Vol 11 (3) ◽  
pp. 177-187 ◽  
Author(s):  
Jerome T. Pearlman ◽  
Frederick Crescitelli ◽  
Nola J. Allston ◽  
Robert J. Petrus ◽  
Jean v.K. Sillman ◽  
...  
Keyword(s):  

2008 ◽  
Vol 50 (4) ◽  
pp. 694-703 ◽  
Author(s):  
Anne L. Escaron ◽  
Michael H. Green ◽  
Sherry A. Tanumihardjo
Keyword(s):  

1986 ◽  
Vol 14 (5) ◽  
pp. 950-950 ◽  
Author(s):  
THERESA C. M. WILSON ◽  
GEORGE A. J. PITT
Keyword(s):  

1962 ◽  
Vol 45 (2) ◽  
pp. 548-561 ◽  
Author(s):  
C. V. Planta ◽  
U. Schweiter ◽  
L. Chopard-dit-Jean ◽  
R. Rüegg ◽  
M. Kofler ◽  
...  

1971 ◽  
Vol 58 (4) ◽  
pp. 351-371 ◽  
Author(s):  
Tom E. Reuter ◽  
Richard H. White ◽  
George Wald

Though it had been supposed earlier that the bullfrog undergoes a virtually complete metamorphosis of visual systems from vitamin A2 and porphyropsin in the tadpole to vitamin A1 and rhodopsin in the adult, the present observations show that the retina of the adult frog may contain as much as 30–40% porphyropsin, all of it segregated in the dorsal zone. The most dorsal quarter of the adult retina may contain 81–89% porphyropsin mixed with a minor amount of rhodopsin; the ventral half contains only rhodopsin. Further, the dorsal zone contains a two to three times higher concentration of visual pigments than the ventral retina. The pigment epithelium underlying the retina contains a corresponding distribution of vitamins A1 and A2, predominantly vitamin A2 in the dorsal pigment epithelium, exclusively vitamin A1 in the ventral zone. The retina accepts whatever vitamin A the pigment epithelium provides it with, and turns it into the corresponding visual pigment. Thus, a piece of light-adapted dorsal retina laid back on ventral pigment epithelium regenerates rhodopsin, whereas a piece of light-adapted ventral retina laid back on dorsal pigment epithelium regenerates predominantly porphyropsin. Vitamin A2 must be made from vitamin A1, by dehydrogenation at the 3,4-bond in the ring. This conversion must occur in the pigment epithelium, presumably through the action of a vitamin A-3,4-dehydrogenase. The essential change at metamorphosis is to make much less of this dehydrogenase, and to sequester it in the dorsal pigment epithelium. Some adult bullfrogs, perhaps characteristically taken in the summer, contain very little porphyropsin—only perhaps 5%—still sequestered in the dorsal retina. The gradient of light over the retinal surface has little if any effect on this distribution. The greater density of visual pigments in the dorsal retina, and perhaps also—although this is less clear—the presence of porphyropsin in this zone, has some ecological importance in increasing the retinal sensitivity to the dimmer and, on occasion, redder light received from below.


1939 ◽  
Vol 22 (6) ◽  
pp. 775-794 ◽  
Author(s):  
George Wald

1. In the rods of fresh-water and some anadromous fishes, rhodopsin is replaced by the purple photolabile pigment porphyropsin. This participates in a retinal cycle identical in form with that of rhodopsin, but in which new carotenoids replace retinene and vitamin A. 2. Porphyropsin possesses a broad absorption maximum at 522 ± 2 mµ, and perhaps a minimum at about 430 mµ. The vitamin A-analogue, vitamin A2, possesses a maximum in chloroform at 355 mµ and yields with antimony trichloride a deep blue color due to a band at 696 mµ. The retinene-analogue, retinene2, absorbs maximally in chloroform at 405 mµ and possesses an antimony chloride maximum at 706 mµ. 3. Its non-diffusibility through a semi-permeable membrane, salting-out properties, and sensitivity to chemical denaturants and to heat, characterize porphyropsin as a conjugated carotenoid-protein. 4. The porphyropsin cycle may be formulated: porphyropsin See PDF for Structure. retinene2-protein (2)→ vitamin A2-protein (3)→ porphyropsin. Isolation of the retina cuts this cycle at (3); denaturation procedures or extraction of porphyropsin into aqueous solution eliminate in addition (1) and (2). 5. The primary difference between the rhodopsin and porphyropsin systems appears to be the possession by the latter of an added ethylenic group in the polyene chain.


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