Purification and partial characterization of a novel cellular retinol-binding protein, type three, from the piscine eyes.
A novel cellular retinol-binding protein, termed type three (CRBP III), was isolated from eyes of the bigeye of tuna. CRBP III showed a molecular weight of 15,400, an isoelectric point of 4.80, alpha 1-mobility in electrophoresis, and a lambda max of 350 nm. All-trans-retinol, the endogenous ligand, could be competitively displaced by retinoic acid but not by retinal. CRBP III was differentiated from purified piscine and rat cellular retinol-binding proteins (CRBP) and cellular retinoic acid-binding proteins (CRABP) by its amino-acid composition, electrophoretic mobility, fluorescence spectra and ligand-binding specificity.
Nishiwaki
S
S
First Department of Internal Medicine, Gifu University School of Medicine, Japan.
Kato
M
M
Okuno
M
M
Kanai
M
M
Muto
Y
Y
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005123:Eye / Q000032:analysis*; D008970:Molecular Weight; D018168:Receptors, Retinoic Acid; D012160:Retina / Q000032:analysis*; D012177:Retinol-Binding Proteins / Q000302:isolation & purification*; D054840:Retinol-Binding Proteins, Cellular; D013050:Spectrometry, Fluorescence; D014413:Tuna
D000596:Amino Acids; D002352:Carrier Proteins; D018168:Receptors, Retinoic Acid; D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular