ISOLATION AND CHARACTERIZATION OF PORCINE MILK LACTOFERRIN

We purified porcine whey lactoferrin by affinity chromatography on a h eparin-Sepharose column, followed by high-performance liquid chromatog raphy. Molecular mass of purified lactoferrin (PLF) is 78,000 daltons. The iron-binding activity of PLF had a UV/visible-light absorption sp ectrum indistinguishable from that of human and bovine lactoferrins (a bsorbance ratio [465 nm/280 nm] approx 0.046). The growth ratio of WIL -2 cells in PLF-supplemented medium is 70% of that in serum-containing medium. The aforementioned characteristics are similar to those of hu man and bovine lactoferrins. Immunoblot analysis, using polyclonal ant ibody raised in rabbits against porcine whey lactoferrin, revealed hig h specificity for PLF, and low cross-reactivity with commercial human and bovine lactoferrins.