Simultaneous purification of biotin-binding proteins-I and -II from chicken egg yolk and their characterization.
Chicken egg yolk biotin-binding protein-I (BBP-I) has been purified to homogeneity along with the tetrameric BBP-II by a common protocol. The purification includes delipidation of egg yolk by butanol extraction, DEAE-Sephacel chromatography, treatment with guanidinium chloride and biotin-aminohexyl-Sepharose affinity chromatography. The identity of purified BBP-I was ascertained by its physicochemical properties as well as by its immunological cross-reactivity and precursor-product relationship with BBP-II.
Subramanian
N
N
Department of Biochemistry, Indian Institute of Science, Bangalore.
Adiga
P R
PR
D000818:Animals; D001710:Biotin / Q000378:metabolism*; D015153:Blotting, Western; D002352:Carrier Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D002645:Chickens; D004527:Egg Proteins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D004530:Egg Yolk / Q000737:chemistry*; D006358:Hot Temperature; D008970:Molecular Weight; D010449:Peptide Mapping
D002352:Carrier Proteins; D004527:Egg Proteins; C017071:biotin-binding proteins; D001710:Biotin