Isolation and characterization of porcine milk lactoferrin

Redman M. Chu From the Department of Pathology, Pig Research Institute, Taiwan, Republic of China, and the Reproduction laboratory, USDAARS, Beltville, MD 20705.

Search for other papers by Redman M. Chu in
Current site
Google Scholar
PubMed
Close
 DVM, PhD
,
Shih-Rong Wang From the Department of Pathology, Pig Research Institute, Taiwan, Republic of China, and the Reproduction laboratory, USDAARS, Beltville, MD 20705.

Search for other papers by Shih-Rong Wang in
Current site
Google Scholar
PubMed
Close
 PhD
,
Chung-Nan Weng From the Department of Pathology, Pig Research Institute, Taiwan, Republic of China, and the Reproduction laboratory, USDAARS, Beltville, MD 20705.

Search for other papers by Chung-Nan Weng in
Current site
Google Scholar
PubMed
Close
 DVM, PhD
, and
Vernon G. Pursel From the Department of Pathology, Pig Research Institute, Taiwan, Republic of China, and the Reproduction laboratory, USDAARS, Beltville, MD 20705.

Search for other papers by Vernon G. Pursel in
Current site
Google Scholar
PubMed
Close
 PhD

Click on author name to view affiliation information

Summary

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.

Summary

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.

All Time Past Year Past 30 Days
Abstract Views 0 0 0
Full Text Views 40 40 6
PDF Downloads 127 127 95
Advertisement