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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 184 (1959), S. 1727-1728 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Alkaline (pH. 8-3-8-8) aqueous digitonin extracts were prepared either from the acid-washed dark-adapted whole retinae2 or from the alum-hardened rods3. The contained visual pigments were then tested for homogeneity by the method of partial bleaching2. Each species was found to possess one visual ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 186 (1960), S. 292-294 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] FOR most practical purposes a thermally stable r compound known as indicator yellow1 is the ultimate product in the bleaching of visual pigments at room temperature. However, irradiated solutions of frog rhodopsin at 3 C.1*2 and of cattle rhodopsin mixed with glycerol at 17 C.3.5 have been ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 178 (1956), S. 860-861 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Solutions of frog visual purple were prepared by the addition of 1 per cent aqueous digitonin solution to whole washed retin . The extracts were buffered to pH 8.0-8.6 by the addition of sodium tetraborate solution. These extracts were then concentrated about 3-4 times in vacuo at low temperature, ...
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 188 (1960), S. 69-69 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Thus irradiation for 1 hr. of frog rhodopsin at ? 5 C. ?generates a mixture of indicator yellow and a stable product with lmax〉 displaced about 20 mm towards the blue. ... At this temperature the photo-product is stable (measurements at 20 mm intervals from 380 to 620 mm interlacing with return ...
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 214 (1967), S. 205-206 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The spectra of Fig. 1 illustrate the results of typical experiments designed to analyse the photopigment content of retinal extracts from fishes representative of the two populations. Absorption spectra for extracts from forma autumnalis had maxima at 511 ±1 nm, identical within experimental ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 212 (1966), S. 1235-1236 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A discharge tube filled with xenon6 was used as a flash source. The recording electrodes were black cotton wicks protruding from black glass pipettes containing 0*9 per cent sodium chloride. The pipettes were bound with black masking tape. Silver wires inserted into these pipettes served as ...
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 221 (1969), S. 275-276 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Twelve albino male Wistar rats (12 weeks old) were dark-adapted for 30 h. Eleven were each injected intraperitoneally with 269 µCi of all-trans retinyl-11,12-3H2-acetate (1.26 mg) and 117 pig of DL-±-tocopherol in 1 ml. of 154 mM sodium chloride containing 15 per cent v/v 'Tween 80' ...
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Human eyes contain an Mr 135K retinol-binding protein that is analogous to interstitial retinol-binding protein (IRBP) in the subretinal space of bovine eyes. It is a glycoprotein, because it binds 125I-concanavalin A, 125I-wheat germ agglutinin and 125I-Lens culinaris hemagglutinin. It does not bind Ricinus communis agglutinin I. After desialation, it binds Ricinus communis agglutinin I, but loses its capacity to bind wheat germ agglutinin. These observations, coupled with the known specificities of these lectins, suggest that at least one of the oligosaccharide chains is a sialated, biantennary complex type containing fucose. Both by direct analysis of dissected ocular tissues and by immunocytochemistry it was shown that human interstitial retinol binding protein is an extracellular protein that is confined predominantly to the subretinal space. Monkey retinas incubated in vitro in medium containing [3H]leucine were shown to synthesize and secrete this protein into the medium, a conclusion that was confirmed by immunoprecipitation with an immunoglobulin fraction prepared from rabbit antibovine IRBP serum. Virtually no other labeled proteins were detectable in the medium. It is concluded that interstitial retinol-binding protein meets many of the requirements for a putative transport protein implicated in the transfer of retinol between the pigment epithelium and retina during the visual cycle, and that the neural retina may play an important role in regulating its amount in the subretinal space.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 195 (1962), S. 40-42 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] ALTHOUGH iodopsin has so far been extracted AJL only from the retina of the chicken, it has been held to be the mediator of photopic vision in a number of vertebrates. Thus, Wald, Brown and Smith1 have written: "... it seems probable that it is the major pigment of cone vision in the frog, snake ...
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 227 (1970), S. 1258-1259 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] One of the earlier methods1 had depended on measurement of the absorbance of retinal oxime produced when a solution of rhodopsin containing liydroxylamine was bleached. From the molar absorbance coefficient of retinal oxime, the corresponding value for rhodopsin was calculated. In private ...
    Type of Medium: Electronic Resource
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