The presence of a novel cellular retinoic acid-binding protein in chick embryos: purification and partial characterization.
Two cellular retinoic acid binding proteins, CRABP I and II, which behaved differently on a DEAE-cellulose column, were purified from 14-day chick embryos. Their molecular weights were 15.8 kDa and 16.2 kDa, respectively. NH2-terminal 36 amino acid sequence of CRABP I was identical to that of bovine CRABP, which was reported previously. CRABP II was a novel cellular retinoic acid binding protein, in which the amino acids at 6 positions of the NH2 terminal sequence are different from those in CRABP I. The homology between CRABP I and II was more than 83%.
Kitamoto
T
T
National Institute of Neuroscience, Tokyo, Japan.
Momoi
T
T
Momoi
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002417:Cattle; D002642:Chick Embryo / Q000032:analysis*; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D018168:Receptors, Retinoic Acid; D012689:Sequence Homology, Nucleic Acid; D013737:Testis / Q000032:analysis; D014212:Tretinoin / Q000378:metabolism
D002352:Carrier Proteins; D018168:Receptors, Retinoic Acid; D014212:Tretinoin