Purification and partial characterization of a cobalamin-binding protein from chicken egg yolk.
Cobalamin-binding protein has been purified from chicken egg yolk by using DEAE-cellulose with a NaCl gradient. The resultant protein fraction was subjected to bioaffinity chromatography. The Mr was 38,000 by SDS-PAGE and 39,000 by gel filtration, and indicated that it was a glycoprotein. The Stokes radius was 4.3 nm and the pI 4.1. The protein bound 57CO.B12 with a molar ratio of 1:1 and a Kd of 0.41 microM. The CBP composed 296 amino acids residues. The protein-ligand interaction was inhibited by Cbl analogues.
Zaman
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K
Department of Animal Biochemistry, Jagiellonian University, Kraków, Poland.
Zak
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Z
D000596:Amino Acids / Q000302:isolation & purification; D000818:Animals; D002642:Chick Embryo; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004530:Egg Yolk / Q000032:analysis*; D006023:Glycoproteins / Q000302:isolation & purification; D014155:Transcobalamins / Q000302:isolation & purification*
D000596:Amino Acids; D006023:Glycoproteins; D014155:Transcobalamins