Separation of large polypeptides by high-performance liquid chromatography

Gazdag, M.; Szepesi, G.

doi:10.1016/s0021-9673(00)82085-3

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1983

1993

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Cited by 22 publications

(3 citation statements)

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“…We have also found that components from previous chromatographic runs can "bleed" from the column and affect the interpretation of the chromatogram. Hancock and Sparrow (1981) 215 nm Gazdag and Szepesi (1981) 210, 230 nrn Harding et al (1981) 210 nm Rivier et al (1977) Fluorescence Rubinstein et al (1977a,b) Lewis et al (1980) . T Hughes et al (1981a,b) Wilson et al (1982a .…”

Section: Detection Systemsmentioning

confidence: 99%

High‐Performance Liquid Chromatography: Analytic and Preparative Applications in Protein‐Structure Determination

Hughes

Wilson

1983

Methods of Biochemical Analysis

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Section: Detection Systemsmentioning

confidence: 99%

High‐Performance Liquid Chromatography: Analytic and Preparative Applications in Protein‐Structure Determination

Hughes

Wilson

1983

Methods of Biochemical Analysis

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“…reversed phase (e.g. Mabichi and Nakahashi, 1981;Gazdag and Szepesi, 1981;Raspi et al, 1990), ion exchange (Mabichi and Nakahashi, 1981;Hefti, 1982) and gel (e.g. Mabichi and Nakahashi, 1981), of high performance liquid chromatography (HPLC) have been applied to aprotinin, there is very little information on aprotinin purity evaluation by HPLC.…”

Section: Introductionmentioning

confidence: 99%

“…According to Gazdag and Szepesi (1981), separation of aprotinin from its impurities can be achieved under conditions which differ from those for the other studied peptides; the pH of the mobile phase is neutral, while for the others its value is below 3. Even at the optimum conditions the separation is not baseline.…”

Section: Introductionmentioning

confidence: 99%

Purity evaluation of aprotinin by high performance liquid chromatography

Dimov¹,

Simeonov²

1993

Biomedical Chromatography

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A separation to the baseline isocratic technique has been developed for the evaluation of the purity of aprotinin by internal normalization. The column used was a 30 nm pore diameter butyl-bonded silica stationary phase. An exact relationship was found to give an adequate description of the retention of aprotinin using acetonitrile concentrations of 17-22% and NaClO4 concentrations of 5-50 mmol. It can be used to optimize the mobile phase content for the particular user column and to compensate for possible variations in the retention time of aprotinin, analysed on different batches of butyl-bonded stationary phases.

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