Plate heights below 50 nm for protein electrochromatography using silica colloidal crystals.

Silica colloidal crystals formed from 330 nm nonporous silica spheres inside of 75 μm i.d. fused silica capillaries were evaluated for the efficiency of capillary electrochromatography of proteins.

Submicrometer plate heights for capillaries packed with silica colloidal crystals.

Extremely uniform packing of colloidal silica in capillaries is shown. Reversed-phase electrochromatograms of DiI-C(12) exhibit plate heights as low as 0.23 microm and a reduced plate height as low as 0.

Separation and analysis of nanomole quantities of heparin oligosaccharides using on-line capillary isotachophoresis coupled with NMR detection.

Glycosaminoglycans (GAGs) are important in a number of biological processes and are structurally altered in many pathological conditions. The complete determination of GAG primary structures has been hampered by the lack of sensitive and specific analytical techniques. Nuclear magnetic resonance spectroscopy (NMR) is a powerful tool for GAG structure elucidation despite its relatively poor limits of detection.