Novel hydrophobic interaction chromatography matrix for specific isolation and simple elution of immunoglobulins (A, G, and M) from porcine serum.

@article{RamosClamont2006NovelHI,
  title={Novel hydrophobic interaction chromatography matrix for specific isolation and simple elution of immunoglobulins (A, G, and M) from porcine serum.},
  author={Gabriela Ramos-Clamont and Maria del Carmen Candia-Plata and Roberto Guzman Zamudio and Luz V{\'a}zquez-Moreno},
  journal={Journal of chromatography. A},
  year={2006},
  volume={1122 1-2},
  pages={28-34}
}
A new, highly acetylated agarose matrix (HA-Sepharose) was synthesized and used as a hydrophobic interaction chromatography (HIC) medium to specifically isolate immunoglobulins (Igs) from porcine serum. Recovery of Igs was in a single step and under mild conditions. HA-Sepharose adsorption was studied in terms of salt, gel acetylation time, flow rate, and protein concentration on the loading buffer. At 0.5 M Na2SO4, control with unmodified Sepharose retained a small fraction (0.70 mg/mL of… CONTINUE READING
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