Separation of mouse immunoglobulins on the basis of water-solubility on Sephadex G-25
| Autor: | M.-C. Savin, H.S. Micklem, H. Bazin |
|---|---|
| Rok vydání: | 1968 |
| Předmět: |
Immunodiffusion
Immunoelectrophoresis Biochemistry Analytical Chemistry chemistry.chemical_compound Mice medicine Methods Animals Solubility Aqueous solution Chromatography medicine.diagnostic_test Elution Organic Chemistry Water Gamma globulin Dextrans General Medicine Phosphate Rats chemistry Distilled water Sephadex Chromatography Gel gamma-Globulins |
| Zdroj: | Journal of chromatography. 34(2) |
| Popis: | Whole mouse serum was placed on columns of Sephadex G-25 “Fine” or “Superfine” equilibrated with distilled water or 0.0001 M phosphate, and eluted with 0.01 M phosphate, pH 7.4, containing 0.15 M NaCl. Proteins were eluted in two peaks. The first emerged in approximately the void volume of the column; the second emerged with and slightly in advance of the salt front. IgM was almost entirely confined to the 2nd peak, which also contained 30–50 % of the IgG, 15–35 % of the IgA, some β-2C and occasionally small amounts of other non-immunoglobulin proteins. Most of the IgA, 50–70 % IgG, and sometimes small traces of IgM appeared in the 1st peak, which also contained the bulk of the non-immunoglobulin proteins. Further purification of the 2nd peak proteins was capable of yielding IgM free of contaminants detectable by immuno-diffusion. The best results were obtained with “Superfine”-grade Sephadex G-25. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|