Evaluation of mass spectrometric techniques for characterization of engineered proteins

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Standard

Evaluation of mass spectrometric techniques for characterization of engineered proteins. / Roepstorff, P; Schram, K H; Andersen, J S; Rafn, K; Baldursson, T; Krøll, J; Poulsen, K; Knudsen, J; Kristiansen, K.

In: Molecular Biotechnology, Vol. 4, No. 1, 1995, p. 1-12.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Roepstorff, P, Schram, KH, Andersen, JS, Rafn, K, Baldursson, T, Krøll, J, Poulsen, K, Knudsen, J & Kristiansen, K 1995, 'Evaluation of mass spectrometric techniques for characterization of engineered proteins', Molecular Biotechnology, vol. 4, no. 1, pp. 1-12. <http://www.ncbi.nlm.nih.gov/pubmed/8521034>

APA

Roepstorff, P., Schram, K. H., Andersen, J. S., Rafn, K., Baldursson, T., Krøll, J., Poulsen, K., Knudsen, J., & Kristiansen, K. (1995). Evaluation of mass spectrometric techniques for characterization of engineered proteins. Molecular Biotechnology, 4(1), 1-12. http://www.ncbi.nlm.nih.gov/pubmed/8521034

Vancouver

Roepstorff P, Schram KH, Andersen JS, Rafn K, Baldursson T, Krøll J et al. Evaluation of mass spectrometric techniques for characterization of engineered proteins. Molecular Biotechnology. 1995;4(1):1-12.

Author

Roepstorff, P ; Schram, K H ; Andersen, J S ; Rafn, K ; Baldursson, T ; Krøll, J ; Poulsen, K ; Knudsen, J ; Kristiansen, K. / Evaluation of mass spectrometric techniques for characterization of engineered proteins. In: Molecular Biotechnology. 1995 ; Vol. 4, No. 1. pp. 1-12.

Bibtex

@article{1e23fdd0a80d11debc73000ea68e967b,
title = "Evaluation of mass spectrometric techniques for characterization of engineered proteins",
abstract = "Mass spectrometric characterization of engineered proteins has been examined using bovine recombinant Acyl-CoA-Binding Protein (rACBP), [15N]-labeled rACBP, and a number of sequence variants of ACBP produced by site-directed mutagenesis. The mass spectrometric techniques include ESIMS and MALDIMS for analysis of the intact protein. Peptide maps have been obtained either by direct analysis of enzymatically derived mixtures by PDMS, ESIMS, and MALDIMS or by off- and on-line HPLC-mass spectrometry. ESIMS was found to be most accurate for analysis of intact proteins. The best sequence coverage in mapping was obtained by LC-ESIMS and by direct mixture analysis by MALDIMS. The latter technique was favorable in terms of sensitivity and speed. A general strategy for mass spectrometric characterization of engineered proteins is suggested.",
author = "P Roepstorff and Schram, {K H} and Andersen, {J S} and K Rafn and T Baldursson and J Kr{\o}ll and K Poulsen and J Knudsen and K Kristiansen",
note = "Keywords: Amino Acid Sequence; Carrier Proteins; Chromatography, High Pressure Liquid; Diazepam Binding Inhibitor; Evaluation Studies as Topic; Lasers; Mass Spectrometry; Molecular Sequence Data; Mutation; Nitrogen Isotopes; Peptide Mapping; Protein Engineering; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization",
year = "1995",
language = "English",
volume = "4",
pages = "1--12",
journal = "Molecular Biotechnology",
issn = "1073-6085",
publisher = "Humana Press",
number = "1",

}

RIS

TY - JOUR

T1 - Evaluation of mass spectrometric techniques for characterization of engineered proteins

AU - Roepstorff, P

AU - Schram, K H

AU - Andersen, J S

AU - Rafn, K

AU - Baldursson, T

AU - Krøll, J

AU - Poulsen, K

AU - Knudsen, J

AU - Kristiansen, K

N1 - Keywords: Amino Acid Sequence; Carrier Proteins; Chromatography, High Pressure Liquid; Diazepam Binding Inhibitor; Evaluation Studies as Topic; Lasers; Mass Spectrometry; Molecular Sequence Data; Mutation; Nitrogen Isotopes; Peptide Mapping; Protein Engineering; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

PY - 1995

Y1 - 1995

N2 - Mass spectrometric characterization of engineered proteins has been examined using bovine recombinant Acyl-CoA-Binding Protein (rACBP), [15N]-labeled rACBP, and a number of sequence variants of ACBP produced by site-directed mutagenesis. The mass spectrometric techniques include ESIMS and MALDIMS for analysis of the intact protein. Peptide maps have been obtained either by direct analysis of enzymatically derived mixtures by PDMS, ESIMS, and MALDIMS or by off- and on-line HPLC-mass spectrometry. ESIMS was found to be most accurate for analysis of intact proteins. The best sequence coverage in mapping was obtained by LC-ESIMS and by direct mixture analysis by MALDIMS. The latter technique was favorable in terms of sensitivity and speed. A general strategy for mass spectrometric characterization of engineered proteins is suggested.

AB - Mass spectrometric characterization of engineered proteins has been examined using bovine recombinant Acyl-CoA-Binding Protein (rACBP), [15N]-labeled rACBP, and a number of sequence variants of ACBP produced by site-directed mutagenesis. The mass spectrometric techniques include ESIMS and MALDIMS for analysis of the intact protein. Peptide maps have been obtained either by direct analysis of enzymatically derived mixtures by PDMS, ESIMS, and MALDIMS or by off- and on-line HPLC-mass spectrometry. ESIMS was found to be most accurate for analysis of intact proteins. The best sequence coverage in mapping was obtained by LC-ESIMS and by direct mixture analysis by MALDIMS. The latter technique was favorable in terms of sensitivity and speed. A general strategy for mass spectrometric characterization of engineered proteins is suggested.

M3 - Journal article

C2 - 8521034

VL - 4

SP - 1

EP - 12

JO - Molecular Biotechnology

JF - Molecular Biotechnology

SN - 1073-6085

IS - 1

ER -

ID: 14639290