Abstract
Lactoperoxidase and lactoferrin were isolated by carboxymethyl cation-exchange chromatography using .05 M phosphate buffer (pH 7.7) and a linear gradient of NaCl from 0 to .55 M. Carboxymethyl-Toyopearl adsorbed only lactoperoxidase and lactoferrin from the albumin fraction of bovine milk acid whey. Lactoperoxidase was released between .10 to .15 M NaCl with a recovery of 91.4%. Lactoferrin was released between .4 to .55 M NaCl and was separated into lactoferrin-a and lactoferrin-b. Yields were 41mg of lactoperoxidase, 21mg of lactoferrin-a, and 67mg of lactoferrin-b as protein from 1L of acid whey. Several minor peaks eluted between 0 to .55M NaCl, and a strong muddy peak was observed during the regenerating phase using .2 N NaOH. The latter peak was estimated as the Ig.
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