Biomedical chromatography : BMC
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Biomed. Chromatogr. · Jun 1999
Chromatographic assay and pharmacokinetic studies of propofol in human serum.
A high-performance liquid chromatographic system with automated precolumn extraction was developed for the determination of propofol in human serum. Propofol of directly injected serum sample was enriched on a protein-coated mu Bondapak phenyl precolumn while serum constituents such as proteins and salts were eluted to waste. Thereafter, using an on-line column-switching system, the drug was quantitatively transferred and separated on a second analytical column followed by spectrophotometric determination at 270 nm. ⋯ The developed method proved to be fast, simple, reproducible, reliable and therefore convenient for propofol monitoring from serum. The recovery of propofol in serum samples from the lowest to the highest concentration ranged from 96.84 to 100.16% (n = 5). The assay was applied to study the pharmacokinetic of the drug in six women undergoing elective caesarean section under general anaesthesia induced with a single intravenous bolus dose of propofol (2.5 mg/kg).
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Biomed. Chromatogr. · Jan 1994
Use of blue-sepharose for purification of immunotoxin containing type 1 ribosome-inactivating protein, gelonin.
This paper describes a method suitable for purifying immunotoxin containing type 1 ribosome-inactivating protein, gelonin. The separation of free (unreacted) 80G, a monoclonal antibody against alpha-fetoprotein (AFP), from semipurified 80G-gelonin conjugate was unsuccessful by conventional CM-Sepharose ion-exchange chromatography because the isoelectric point of the conjugate did not increase enough to reach that of gelonin alone. ⋯ However, a small amount of conjugate containing gelonin modified with N-succinimidyl 3-(2-pyridyldithio)propionate, but not with 2-iminothiolane, could not bind to the column. The conjugate purified by the use of Blue Sepharose showed selective cytotoxicity against AFP-producing human hepatoma cells.
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Biomed. Chromatogr. · Jan 1987
Computerized chromatographic peak detection using the trigg tracking signal. An application devised for use with an online analog to digital converter connected between an amino acid analyser and a personal computer.
Manual integration of the amino acid peaks from physiological samples produced by conventional anion exchange liquid chromatography is a time-consuming process. This paper describes a combined unit, consisting of an analog to digital converter and a personal computer, which was connected in parallel with the chart recorder and the analyser's 570 nm channel of the colorimeter. The computer was programmed to log the digitized data, detect the start, maximum and end of each chromatographic peak, calculate the area under the peak and its retention time and provide a printout of the results at the end of the elution program. ⋯ This approach proved to have an equivalent performance to the manual method for 17 out of the 19 amino acids normally quantitated in physiological samples. The automated detection and quantitation of arginine was unsatisfactory due to its characteristically low profile peak shape, and proline was not measured because the device was not connected to the 440 nm channel of the colorimeter. The automated system provided economic and analytically acceptable solutions to the problem of providing an online integrator versatile enough to be used with the 255 min long amino acid analysis of physiological fluids.