Affinity chromatography of serum albumin with fatty acids immobilized on agarose.

摘要: Abstract Fatty acids immobilized on agarose have been employed in the isolation and study of serum albumin by affinity chromatography. Various oleyl- palmityl-aminoalkyl-amino-agarose preparations bound about 10 mg per ml agarose; other proteins were retained smaller amounts with lesser affinity. acid-agarose columns which had exposed to human then washed yielded essentially pure upon elution 50% alcohol at pH 3. Lengthening aminoalkylamino "arm" from 2 carbon atoms little effect capacity for albumin, but increased binding proteins. That was caused fatty shown use control without acids, inverse relation acid content ability elute solutions sodium oleate. Efforts made isolate regions bovine molecule after tryptic digestion acid-agarose. Two peptides molecular weight 10,000 23,000 obtained resistant further digestion; larger these purified its amino composition determined. This peptide lacked cysteine tryptophan, apparently arises carboxyl-terminal portion molecule. Some implications properties acid-binding sites offered.