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Sepharose ionic strength effect

In gel filtration the buffer has little effect on the elution of the proteins in the sample and the limitations are imposed by the stability of the matrix. Sepharose is stable within the pH range of 4.0-9.0, CL-Sepha-rose, between pH values of 3.0 and 14.0, and Sephaciyl from pH 3.0-11.0. There is the possibility of some ionic interaction between the matrix and the protein at very low ionic strength and therefore it is usual to maintain a salt concentration of approx 0.1-0.15 M to prevent this. [Pg.227]

Figure 3. Effect of ionic strength on dissociation constant, K Figure 3. Effect of ionic strength on dissociation constant, K<j, for lysozyme and bovine serum albumin on Cibacron Blue Sepharose CL-4B [6],...

See other pages where Sepharose ionic strength effect is mentioned: [Pg.33]    [Pg.241]    [Pg.135]    [Pg.16]    [Pg.132]    [Pg.333]    [Pg.266]    [Pg.160]    [Pg.261]   


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