Evaluation of cation exchange chromatography for the isolation of M glycoprotein from histoplasmin.

@article{ZancopOliveira1993EvaluationOC,
  title={Evaluation of cation exchange chromatography for the isolation of M glycoprotein from histoplasmin.},
  author={Rosely Maria Zancop{\'e}-Oliveira and Sandra L. Bragg and Steven F. Hurst and Jos{\'e} Mauro Peralta and E. Rei\ss},
  journal={Journal of medical and veterinary mycology : bi-monthly publication of the International Society for Human and Animal Mycology},
  year={1993},
  volume={31 1},
  pages={29-41}
}
Cation exchange chromatography was evaluated to purify the M antigen from histoplasmin (HMIN). Two H and M antigen-containing fractions, soluble (S) and precipitate (PP), resulted from the initial 0.025 M, pH 3.5 citrate buffer dialysis step. The PP fraction contained 62% of the M antigen activity and was resolubilized. Both fractions were chromatographed on CM Sepharose CL-6B. Polysaccharide C antigen was abundant in the S fraction and most of it did not bind to CM Sepharose. M antigen… CONTINUE READING

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