Interphotoreceptor Retinoid-binding Protein
نویسندگان
چکیده
منابع مشابه
Interphotoreceptor Retinoid Binding Protein; Myths and Mysteries
Although it is the major soluble protein component of the extracellular matrix bathing the photoreceptors, little is known about the structure and function of interphotoreceptor retinoid-binding protein (IRBP). The critical anatomic compartment it occupies cannot be overemphasized as through the involution of the optic vesicle, the retinal pigmented epithelium (RPE) comes in contact with the ne...
متن کاملNormal cone function requires the interphotoreceptor retinoid binding protein.
11-cis-retinal is the light-sensitive component in rod and cone photoreceptors, and its isomerization to all-trans retinal in the presence of light initiates the visual response. For photoreceptors to function normally, all-trans retinal must be converted back into 11-cis-retinal through a series of enzymatic steps known as the visual cycle. The interphotoreceptor retinoid-binding protein (IRBP...
متن کاملProperties of an interphotoreceptor retinoid-binding protein from bovine retina.
Washes and extracts of frozen and fresh cattle retina contain a water-soluble high-molecular-weight, retinoid-binding protein that is distinct from three other retinoid-binding proteins previously isolated from this tissue. The protein can be purified to apparent homogeneity from retinal homogenates by a combination of gel filtration, lectin, and ion-exchange chromatography. Overestimation of t...
متن کاملInterphotoreceptor retinoid-binding protein promotes rhodopsin regeneration in toad photoreceptors.
Interphotoreceptor retinoid-binding protein (IRBP) has been hypothesized to function as an intercellular shuttle in the vertebrate eye, serving to transport retinoids between the retinal pigment epithelium (RPE) and photoreceptors in the process by which visual pigment is regenerated after photolysis. This hypothesis was tested in preparations utilizing the toad (Bufo marinus) eye and purified,...
متن کاملThiol-dependent antioxidant activity of interphotoreceptor retinoid-binding protein.
Interphotoreceptor retinoid-binding protein (IRBP), which is critical to photoreceptor survival and function, is comprised of homologous tandem modules each ∼300 amino acids, and contains 10 cysteines, possibly 8 as free thiols. Purification of IRBP has historically been difficult due to aggregation, denaturation and precipitation. Our observation that reducing agent 1,4-dithiothreitol dramatic...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85061-5