Isolation, Purification, and Molecular Weight Determination of Serum Immunoglobulin from Gulf Menhaden: Development of an Enzyme-Linked Immunosorbent Assay to Assess Serum Immunoglobulin Concentrations from Atlantic Menhaden.

@article{Shelby2002IsolationPA,
  title={Isolation, Purification, and Molecular Weight Determination of Serum Immunoglobulin from Gulf Menhaden: Development of an Enzyme-Linked Immunosorbent Assay to Assess Serum Immunoglobulin Concentrations from Atlantic Menhaden.},
  author={Richard Allen Shelby and Joyce J. Evans and Phillip H. Klesius},
  journal={Journal of aquatic animal health},
  year={2002},
  volume={14 4},
  pages={
          254-262
        }
}
An immunoglobulin M (IgM)-like immunoglobulin was isolated by polyethylene glycol precipitation from pooled serum collected from healthy gulf menhaden Brevoortia patronus. The immunoglobulin (Ig) was purified by Sephacryl-400 gel filtration chromatography. The molecular weight of unreduced, purified Ig was determined to be 850 kilodaltons (kD) by high-performance liquid chromatography. A goat antiserum against the purified Ig was produced and determined to react with the serum Ig of both gulf… CONTINUE READING
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