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Journal of Dairy Science Vol. 74 No. 2 404-408
© 1991 by American Dairy Science Association ®
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Interacting Properties of Bovine Lactoferrin with Immobilized Cibacron Blue F3GA in Column Chromatography

Kei-Ichi Shimazaki 1 and Naoto Nishio 1

1 Dairy Chemistry Research Laboratory, Bioindustrial Chemistry Department, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido, 080 Japan

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.

Key Words: lactoferrin • Cibacron blue • affinity chromatography

Submitted on July 6, 1989
Accepted on August 31, 1990






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Copyright © 1991 by the American Dairy Science Association ®.