Distribution of interstitial retinol-binding protein (IRBP) in the vertebrates.

Simple item page
dc.acquisition-srcen_US
dc.call-noAcc# 3063en_US
dc.contract-noen_US
dc.contributor.authorBridges, C.D.B.en_US
dc.contributor.authorLiou, G.I.en_US
dc.contributor.authorAlvarez, R.A.en_US
dc.contributor.authorLanders, R.A.en_US
dc.contributor.authorLandry, A.M., Jr.en_US
dc.contributor.authorFong, S.L.en_US
dc.contributor.otherJournal of Experimental Zoology.en_US
dc.date.accessioned2010-02-15T17:00:10Z
dc.date.available2010-02-15T17:00:10Z
dc.date.issued1986en_US
dc.degreeen_US
dc.descriptionp. 335-346.en_US
dc.description-otheren_US
dc.description.abstractImmunoblots of interphotoreceptor matrix preparations from 20 species belonging to six vertebrate classes were probed with antibodies against bovine interstitial retinol-binding protein (b-IRBP). Each preparation displayed an immunoreactive protein band. In the Osteichthyes, the apparent Mr of this band was 67,600 +/- 2,700 (x +/- SD, n=8). In two of the Osteichthyes, the band was resolved into a closely spaced doublet. Including previously published data for five mammals and one amphibian, species from the other classes (Chondrichthyes, one species; Amphibia, four species; Reptilia, one species; Aves, one species; Mammalia, nine species) had IRBPs with Mr that averaged 2.0 times that of the Osteichthyes, namely 134,200 +/- 8,600 (x +/- SD, n= 17). Frog IRBP was very similar to mammalian IRBP in terms of its immunohistochemical distribution (determined with rabbit anti-frog IRBP antibodies), its molecular weight (sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel-filtration chromatography), retinol- and concanavalin A-binding ability, and because it was synthesized and secreted in vitro by the isolated retina but not by the pigmented layers of eye. Goldfish IRBP apparently binds exogenous (3H)-retinol but does not bind concanavalin A and has about half the Mr of frog IRBP. The occurrence of IRBP-like proteins cross-reacting with anti b-IRBP antibodies in the interphotoreceptor matrix of all six major vertebrate classes is consistent with the hypothesis that IRBP is an important element in the vertebrate visual cycle.en_US
dc.description.urihttp://gbic.tamug.edu/request.htmen_US
dc.geo-codeTexas coasten_US
dc.historyen_US
dc.identifier.urihttp://hdl.handle.net/1969.3/20869
dc.latitudeen_US
dc.locationGBIC Collectionen_US
dc.longitudeen_US
dc.notesen_US
dc.placeen_US
dc.publisheren_US
dc.relation.ispartofseries3063.00en_US
dc.relation.urien_US
dc.scaleen_US
dc.seriesen_US
dc.subjectvertebrate zoologyen_US
dc.subjectproteinsen_US
dc.subjecteyesen_US
dc.titleDistribution of interstitial retinol-binding protein (IRBP) in the vertebrates.en_US
dc.typeArticleen_US
dc.universityen_US
dc.vol-issue239en_US

Files

Collections

Galveston Bay Bibliography
GBIC Materials Available at Jack K. Williams Library