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Retinochrome and rhodopsin in the extraocular photoreceptor of the squid, Todarodes.
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The deep-sea squid, Todarodes pacificus, possesses well-developed parolfactory vesicles as extraocular photoreceptors connected with the brain. The ventral set of vesicles forms a thread approximately 3mm long and looks orange owing to photopigments. The vesicle mainly consists of receptor cells, each of which is similar in structure to the visual cell, carrying rhabdomeres in the distal process and lamellated myeloid bodies in the proximal part. Recently we noticed that a crude extract of the vesicles is capable of isomerizing retinal from all-trans to the 11-cis form in the light, and confirmed that the vesicles in fact contained retinochrome in addition to rhodopsin. This is the first time that retinochrome has been detected in any place other than ocular tissues. The optical and chemical nature of these photopigments is the same as that we have observed in the Todarodes retina. Quantitative extractions have shown that the total yield of photopigments is approximately 0.0006 in absorbance at lambda max (light path, 10 mm) per milliliter per thread of vesicles, and that the amount of retinochrome in the vesicles is roughly equivalent to that of rhodopsin. Whereas rhodopsin is located in the rhabdomal membranes, retinochrome is probably associated with lamellated structures and their derivatives in the cytoplasm. In the parolfactory vesicles, retinochrome may also cooperate with rhodopsin in the same way as has been discussed for retinal photoreception.
Title: Retinochrome and rhodopsin in the extraocular photoreceptor of the squid, Todarodes.
Description:
The deep-sea squid, Todarodes pacificus, possesses well-developed parolfactory vesicles as extraocular photoreceptors connected with the brain.
The ventral set of vesicles forms a thread approximately 3mm long and looks orange owing to photopigments.
The vesicle mainly consists of receptor cells, each of which is similar in structure to the visual cell, carrying rhabdomeres in the distal process and lamellated myeloid bodies in the proximal part.
Recently we noticed that a crude extract of the vesicles is capable of isomerizing retinal from all-trans to the 11-cis form in the light, and confirmed that the vesicles in fact contained retinochrome in addition to rhodopsin.
This is the first time that retinochrome has been detected in any place other than ocular tissues.
The optical and chemical nature of these photopigments is the same as that we have observed in the Todarodes retina.
Quantitative extractions have shown that the total yield of photopigments is approximately 0.
0006 in absorbance at lambda max (light path, 10 mm) per milliliter per thread of vesicles, and that the amount of retinochrome in the vesicles is roughly equivalent to that of rhodopsin.
Whereas rhodopsin is located in the rhabdomal membranes, retinochrome is probably associated with lamellated structures and their derivatives in the cytoplasm.
In the parolfactory vesicles, retinochrome may also cooperate with rhodopsin in the same way as has been discussed for retinal photoreception.
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