[Isolation of cellular retinol-binding protein from cattle liver].
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.
Chetyrkin
S V
SV
Chernukhina
L A
LA
Donchenko
G V
GV
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
D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular
Vydelenie kletochnogo retinolsviazyvaioshchego belka iz pecheni byka.