title: [Isolation of cellular retinol-binding protein from cattle liver].
abstract: Cellular retinol-binding protein from bovine liver has been purified to homogeneity. The protein binds retinol with high affinity; the apparent dissociation constant was determined by fluorometric titration to be 2.18 x 10(-3) M. Retinol bound to the protein has an absorption spectrum (lambda max = 350 nm) and considerably differs from the spectrum of retinol absorption in ethanol (lambda max = 325 nm). The protein is a single polypeptide chain with a molecular weight of approximately 14 kDa based on information obtained by sodium dodecyl sulfate-polyacrylamide electrophoresis.
authors.forename: S V
authors.initials: SV
authors.lastname: Chetyrkin
authors.forename: L A
authors.initials: LA
authors.lastname: Chernukhina
authors.forename: G V
authors.initials: GV
authors.lastname: Donchenko
mesh_terms: D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000737:chemistry* / Q000166:cytology; D008970:Molecular Weight; D011485:Protein Binding; D012177:Retinol-Binding Proteins / Q000302:isolation & purification*; D054840:Retinol-Binding Proteins, Cellular; D013056:Spectrophotometry, Ultraviolet; D017186:Titrimetry
chemical_list: D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular
vernacular_title: Vydelenie kletochnogo retinolsviazyvaioshchego belka iz pecheni byka.