Sentence examples for using a linear acetonitrile from inspiring English sources

Chromatography was performed on a LC Packings HPLC with a C18 PepMap column (Dionex, Sunnyvale, CA) using a linear acetonitrile gradient and 200 nL/min flow rate.

Peptides were purified by preparative reverse-phase HPLC on a C8 column, using a linear acetonitrile gradient in an aqueous solution of 0.1% (v/v) trifluoroacetic acid.

Peptides were purified by preparative reverse-phase HPLC on a C8 column using a linear acetonitrile gradient in a TFA aqueous solution 0.1% (v/v).

Cleavage from the resin and removal of protecting groups was effected by a mixture of trifluoroacetic acid (95%), triisopropylsilane (2.5%) and water (2.5%).Peptides were purified by reverse-phase liquid chromatography using a linear acetonitrile:water gradient and masses were verified by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry.

The various forms of vitamin B12 in cytosolic and mitochondria enriched fractions were analysed by HPLC as described [8]. the method was adapted from Miller et al. [34] as described [35] and is based on a reverse phase high performance liquid chromatography technique using a linear acetonitrile gradient.

The RP separation was performed using a linear acetonitrile gradient from 99% buffer A (100% D.I. water/0.1% formic acid) to 85% buffer B (100%acetonitrile/0.1%% formic acid) in 45 min using the micropump.

Tryptic digests of C. butyricum for MRM experiments (QTRAP 5500) were separated using a linear 0.87% acetonitrile per minute gradient (0.4-37.4% acetonitrile in 42.5 min) followed by washing and equilibration steps.

The results showed that satisfactory separation could best be obtained by eluting DB samples on a BEH C18 column at 40°C using a linear gradient of acetonitrile and water within 15 min. A wavelength of 280 nm was chosen to monitor the analytes after comparing the chromatograms of the DB samples recorded at wavelengths within 190 500 nm.

and the peptides were chromatographed using a linear gradient of acetonitrile from 6% to 50% in aqueous 0.1% formic acid over 50 minutes at the 25 µL/min flow rate.

After the washing step, the trapping column was switched in-line with a reversed-phase C18 Acclaim PepMap 100 column (0.075×150 mm, Dionex) and the peptides were chromatographed using a linear gradient of acetonitrile from 2% to 50% in aqueous 0.1% formic acid over a period of 40 min at 300 nL/min and the eluate was directly introduced into the mass spectrometer.

Trapped peptides were then eluted onto a reversed-phase PicoFrit column (New Objective) using a linear gradient of acetonitrile (0 60%) containing 0.1% FA.