Isolation and characterization of porcine milk lactoferrin

Chu, R.M.; Wang, S.R.; Weng, C.N.; Pursel, V.G.

Isolation and characterization of porcine milk lactoferrin

1993

Chu, R.M. | Wang, S.R. | Weng, C.N. | Pursel, V.G.

We purified porcine whey lactoferrin by affinity chromatography on a heparin-sepharose column, followed by high-performance liquid chromatography. Molecular mass of purified lactoferrin (PLF) is 78,000 daltons. The iron-binding activity of PLF had a UV/ visible-light absorption spectrum indistinguishable from that of human and bovine lactoferrins (absorbance 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 human and bovine lactoferrins. Immunoblot analysis, using polyclonal antibody raised in rabbits against porcine whey lactoferrin, revealed high specificity for PLF, and low cross-reactivity with commercial human and bovine lactoferrins.

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AGROVOC Keywords

animals antibodies chemistry chromatography electrophoresis immunoblotting iron isolation kinetics lactoferrin lactoferrin metabolism milk molecular weight swine whey

Bibliographic information

Published in

American journal of veterinary research

Volume 54 Issue 7 Pagination 1154 - 1159 ISSN 0002-9645

Other Subjects

Characterization; High pressure liquid; Female; Cell growth; Polyacrylamide gel; Isolation & purification; Iron binding capacity; Sow milk; Enzyme-linked immunosorbent assay

Language

English

Note

2019-12-05

Type

Text; Journal Article

In AGRIS since: 2024-02-28

Format: MODS

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