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At least 325 records · Page 18Linked to original sources
PubMed1990

High-performance affinity chromatography of DNA.

The octadecamer of thymidylic acid, (dT)18, was synthesized with a primary amino group on the 5'-terminal phosphate and this was covalently coupled to 300 A pore macroporous silica. Coupling was performed inside a prepacked column to an activated N-hydroxysuccinimidyl ester silica. The (dT)18-silica column successfully separates mixtures of adenine oligomers differing in length by one nucleotide. The dependence upon salt concentration, temperature and length for elution of oligonucleotides was determined. Methods were also developed to selectively elute such columns using either salt or temperature gradients.

Cation Exchange Resins↗
PubMed1986

Combined use of trypsin-agarose affinity chromatography and reversed-phase high-performance liquid chromatography for the purification of single-chain protease inhibitor from corn seeds.

We have developed a large-scale method for recovering the corn inhibitor of trypsin and activated Hageman factor from a trypsin-agarose column predominantly in the single-chain form. To do so, inhibitor retained by the column was eluted with 1.0 M glycine buffer, pH 2.1. We have used reversed-phase high-performance liquid chromatography to further purify the inhibitor eluted from the trypsin-agarose column by separating the single-chain inhibitor from two-chain inhibitor (a small amount of which is present in the preparation after trypsin-agarose chromatography) and from still smaller amounts of another protein (apparently trypsin) that appears as a contaminant during trypsin-agarose chromatography.

Amino Acids↗
PubMed1990

Tresyl-activated support for high-performance affinity chromatography.

A new activated support TSK gel Tresyl-5PW was evaluated for the coupling of antibodies, which was found to occur easily under mild conditions with high yields. Optimum coupling conditions were a 2-h reaction at 25 degrees C in 1 M phosphate buffer (pH 7.5) when 2-3 mg antibody/ml support is to be coupled and a 6-7-h reaction when ca. 10 mg antibody/ml support is to be coupled. When antibodies were coupled under these conditions, antibody coupling yields greater than 80% and antigen binding efficiencies of 70-80% were achieved, probably owing to a selective attachment of the Fc region of the antibodies. Antigens (human serum proteins) could be separated rapidly without denaturation on antibody-coupled Tresyl-5PW.

Antibodies↗
PubMed2003

Aptamer affinity chromatography for rapid assay of adenosine in microdialysis samples collected in vivo.

An anti-adenosine aptamer was evaluated as a stationary phase in packed capillary liquid chromatography. Using an aqueous mobile phase containing 20 mM Mg2+, adenosine was strongly retained on the column. A gradient of increasing Ni2+ (to 18 mM), which is presumed to complex with nitrogen atoms in adenosine involved in binding to the aptamer, eluted adenosine in a narrow zone. Up to 6 microl of 1.2 microM adenosine could be injected onto the 150-microm I.D. x 7 cm long column without loss of adenosine. With UV absorbance detection, the detection limit was 30 nM or 120 fmol (4 microl injected). Samples could be repetitively injected with 4.6% relative standard deviation in peak area. Columns were stable to at least 200 injections. The adenosine assay, which required no sample preparation, was used on microdialysis samples collected from the somatosensory cortex of chloral hydrate anesthetized rats. Total analysis times were short enough that dialysate samples could be injected every 5 min. Basal dialysate concentrations of adenosine stabilized at 87+/-10 nM (n=5) with the probe operated at 0.6 microl/min.

Adenosine↗