Sephacryl Gels: Physical Properties and Evaluation of Performance in Gel Filtration
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1978
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Sephacryl is a gel filtration medium composed of allyl dextran and N2N1-methylene bisacrylamide. Sephacryl S-200 SF has a fractionation range similar to that of Sephadex G-150. Sephacryl S-300 SF has a fractionation rangernore similar to Sephadex G-200 or Sepharose 68, with an exclusion limit fbr globular proteins of about loE daltons. In typical applications, excellent resolution of protein mixtures was obtained at flow rates up to 30 cm/hr. Good correlation was established between elution volumes of proteins and their molecular weights. The gels contain feu ionic groups, as determined by titration. Studies using Sephacryl S-200 at different pH values indicate that, above pH 3, protein does not interact with Sephacryl S-200 at moderate ionic strengths. However, below pH 3, protein binds strongly to the gel through hydrophobic interactions and/or hydrogen bonding. Most separations using Sephadex 6-150 or Sephadex G-200 could be duplicated using Sephacryl S-200 or S-300 at much higher flow rates.
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Journal of Liquid Chromotography, 1(6), 811-832, 1978