Author Wang's current address: Dept. of Food & Nutrition, Providence Univ., Shalu, Taiwan.
Milk Alkaline Phosphatase Purification and Production of Polyclonal Antibodies
Article first published online: 20 JUL 2006
Journal of Food Science
Volume 64, Issue 4, pages 601–605, July 1999
How to Cite
Vega-Warner, A. V., Wang, C.-H., Smith, D. M. and Ustunol, Z. (1999), Milk Alkaline Phosphatase Purification and Production of Polyclonal Antibodies. Journal of Food Science, 64: 601–605. doi: 10.1111/j.1365-2621.1999.tb15093.x
The financial support of the Michigan Agricultural Experiment Station and State of Michigan Crop and Food Bioprocessing Center is gratefully acknowledged.
- Issue published online: 20 JUL 2006
- Article first published online: 20 JUL 2006
- MS #3488. Received 8/7/98; revised 1/26/99; accepted 2/9/99.
- alkaline phosphatase;
Purification was by electroelution from native polyacrylamide gels or by sequential use of three columns. Electroelution was faster and resulted in a higher yield (23.4 vs 1.6%) than column purification. The enzyme had a molecular mass of 187 kDa, and the isoelectric point ranged from 5.4 to 6.0. ALP purified by electroelution was used as the antigen to immunize rabbits for polyclonal antibody (PAb) production. Western blot analysis showed that PAbs cross-reacted with bovine milk and placenta ALP, but did not cross-react with ALP from calf or bovine intestinal mucosa, Escherichia coli or with other milk proteins.