Abstract
Bovine lactoferrin, isolated from colostral milk, interacted strongly with immobilized Cibacron blue F3GA column. Lactoferrin, adsorbed on the dye column, could not be eluted by 8 M urea, 1% Triton X-100, and 75% ethylene glycol, but was eluted by .1 M sodium hydroxide, 1 M potassium thiocyanate, 3 M potassium chloride and free Cibacron blue F3GA. Electrostatic forces between the sulfonic groups of Cibacron blue F3GA and the basic side-chain groups in lactoferrin molecule probably are responsible for the observed interaction. The elution profile for lactoferrin differed from those of lactoperoxidase and serum albumin, which might allow efficient isolation of lactoferrin from whey via affinity chromatography.
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