A biochemical characterisation of the photophore lenses of Porichthys notatus Girard

Dove, S., Horwitz, J. and McFall-Ngai, M. (1992) A biochemical characterisation of the photophore lenses of Porichthys notatus Girard. Journal of Comparative Physiology A: Neuroethology, Sensory, Neural, and Behavioral Physiology, 172 5: 565-565.


Author Dove, S.
Horwitz, J.
McFall-Ngai, M.
Title A biochemical characterisation of the photophore lenses of Porichthys notatus Girard
Formatted title A biochemical characterization of the photophore lenses of the midshipman fish, Porichthys notatus Girard
Journal name Journal of Comparative Physiology A: Neuroethology, Sensory, Neural, and Behavioral Physiology   Check publisher's open access policy
ISSN 0340-7594
1432-1351
Publication date 1992-05
Sub-type Article (original research)
DOI 10.1007/BF00213679
Volume 172
Issue 5
Start page 565
End page 565
Total pages 572
Editor 8
Place of publication Berlin, Germany
Publisher Springer
Language eng
Subject 060112 Structural Biology (incl. Macromolecular Modelling)
060809 Vertebrate Biology
Formatted abstract The present study is a biochemical characterization of the photophore lenses of the midshipman fish, Porichthys notatus, a species that bears 800 photophores distributed over the body surface. The biochemical properties of the photophore lenses were compared with those of the eye lens with which they share a similar developmental origin and analogous function. To achieve a high refractive index, the vertebrate eye lens has a relatively high concentration of structural proteins (20–50%, depending on species) and a simple protein composition, that is, relatively few proteins are synthesized in comparison to other tissues. Similarly, the photophore lenses of P. notatus had a relatively high protein concentration (average = 29%, n = 5) and approximately 60% of the total soluble protein was represented by two subunit species of 33 kD and 35 kD on denaturing polyacrylamide gels. The structural proteins of the eye lens are of two principle types: 1)  beta and gamma polypeptides which belong to vertebrate lens-specific crystallin families, and, 2) enzymes recruited into the lens which take on the function of structural proteins. Here, we report that the two major photophore lens subunits of 33 kD and 35 kD are biochemically similar to each other, but are clearly distinct from any of the previously characterized crystallins. Therefore, we propose that photophore lenses appear to recruit a novel protein.
Keyword Photophore
Lens
Crystallin
Porichthys
Midshipman
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Centre for Marine Studies Publications
 
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