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Three monoliths based on  poly (glycidyl methacrylate- co -divinylbenzene) were prepared in the confines of borosilicate glass columns (100 × 3 mm I.D.). The first monolith was applied for analysis of proteins by reversed-phase high-performance liquid chromatography. It furnished a fast base-line separation for four proteins (ribonuclease A, cytochrome  c ,  α -lactalbumin and myoglobin) in &lt;80 s, with optimum resolution range of 2.11–2.84, and extremely small values of peak width at half height with a range of 1.0–1.6 s. The second and third monoliths were surface-modified into weak and strong anion-exchangers, respectively, and were investigated for anion-exchange (AE) high-performance liquid chromatography of four proteins with acidic isoelectronic points (bovine carbonic anhydrase, conalbumin, ovalbumin and soybean trypsin inhibitor) and of 5-phosphorylated oligodeoxythymidylic acids fragments [d(pT) 12–18 ]. The weak AE monolith experienced complete elution of the four proteins applying a basic Tris–HCl buffer (0.02 M, pH 8.9); however, the strong AE monolith established a base-line separation of these proteins in ~14 min. Both monoliths showed base-line separation of the seven fragments of d(pT) 12–18  in ~6 min. The ion-exchange capacity determined by frontal and elemental analyses was comparable for the weak AE monolith (0.75 and 0.80 meq/g) and for the strong AE monolith (0.81 and 0.87 meq/g), respectively. Finally, a run-to-run and monolith-to-monolith reproducibility showed a relative standard deviation in retention time of d(pT) 12–18  fragments of &lt;2%.

journal of chromatographic science

Wide-Bore Columns of  Poly (Glycidyl Methacrylate- Co -Divinylbenzene)-Based Monolithic Beds for Reversed-Phase and Anion-Exchange Chromatographic Separation of Biomolecules