Capillary zone electrophoresis of peptide fragments from trypsin digestion of biosynthetic human growth hormone

Nielsen, R.G.; Riggin, R.M.; Rickard, Eugene C.

doi:10.1016/s0021-9673(01)84308-9

Cited by 69 publications

(10 citation statements)

References 11 publications

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“…Peptide maps have also been used for determining changes in oxidation, deamidation, and the primary sequence of proteins by HPLC. CZE was used to generate a peptide map of recombinant growth hormone (rhGH, [47]). CZE displayed an advantage over HPLC in greater throughput of samples and a decrease in analysis time.…”

Section: Reviews Of Ce Used For the Analysis Of Recombinant Proteinsmentioning

confidence: 99%

Capillary Electrophoresis in the Development of Recombinant Protein Biopharmaceuticals

Chen¹,

Canova-Davis²

2001

CE in Biotechnology: Practical Applications for Protein and Peptide Analyses

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The understanding of the physicochemical properties of proteins in solution is required to understand the separations taking place in the capillary. For example, during isoelectric focusing, it is important to ensure the lack of protein precipitation during fOCUSing and mobilization otherwise artifacts occur and the true resolution of charge variants is not achieved. Similarly, buffer conditions, including additives, composition of buffer, and pH can influence the resolution of product variants. With diligent efforts one can achieve desired separations. As knowledge of buffer conditions and use of these techniques increase, the methods will be improved.MECC can be useful for the characterization of recombinant proteins and monoclonal antibodies. However, the relatively long analyte migration times may be a deterrent for routine use in quality control situations. Pharmaceutical companies will employ new techniques which provide advantages over current technology. CE has advantages in certain applications. Applications which use slab gel techniques, IEF and SDS-PAGE can be replaced by the CE methods for formulation development, characterization of charge isoforms, and for purity determinations. CZE and clEF can be used for rapid identity tests which do not require peptide mapping. CZE has a tremendous advantage in analyzing basic proteins, and CZE and CE-SDS can be used to quantify product in the presence of interfering excipients. It is the responsibility of the analytical chemist to determine applications which are appropriate for CEo It is apparent that these are currently being defined for the biotechnology industry, and the usage of CE should continue to increase.

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Section: Reviews Of Ce Used For the Analysis Of Recombinant Proteinsmentioning

confidence: 99%

Capillary Electrophoresis in the Development of Recombinant Protein Biopharmaceuticals

Chen¹,

Canova-Davis²

2001

CE in Biotechnology: Practical Applications for Protein and Peptide Analyses

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show abstract

“…This phenomenon seemed specific to diamino structure because the corresponding monoamino compounds were not effective. 1,4-diaminobutane, 1,5-diaminopentane, and 1,3-diaminopropane have beenused for this purpose [117,118].…”

Section: Organic Modifiersmentioning

confidence: 99%

Capillary electrophoresis separation of neutral organic compounds, pharmaceutical drugs, proteins and peptides, enantiomers, and anions

Ding

1999

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“…It has been shown that CE can provide information on identity, purity, and structural changes of peptides [8][9][10][11]. In recent years, CE-MS coupling has become an important if not indispensable tool in this field of research [12][13][14][15][16][17][18][19][20].…”

Section: Introductionmentioning

confidence: 99%

Capillary electrophoresis‐mass spectrometry of peptides from enzymatic protein hydrolysis: Simulation and optimization

Simó

Cifuentes

2003

Electrophoresis

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Two important limitations still exist for the characterization of protein digests by capillary electrophoresis-mass spectrometry (CE-MS): (i) the buffer choice (i.e., the buffer must provide an adequate CE separation without ruining the MS signal), and (ii) the frequent generation of "unexpected" peptidic fragments during the enzymatic protein hydrolysis. In this work, a new approach is used to solve these difficulties, namely a theoretical model that relates the electrophoretic behavior of peptides to their sequence. The effectiveness of this procedure is demonstrated by the fast attainment of good CE-MS conditions for analyzing the peptides obtained from an enzymatic protein hydrolysate in a single run. This strategy can provide useful information for helping to characterize "unexpected" fragments from protein digests.

show abstract

Capillary zone electrophoresis of peptide fragments from trypsin digestion of biosynthetic human growth hormone

Cited by 69 publications

References 11 publications

Capillary Electrophoresis in the Development of Recombinant Protein Biopharmaceuticals

Capillary Electrophoresis in the Development of Recombinant Protein Biopharmaceuticals

Capillary electrophoresis separation of neutral organic compounds, pharmaceutical drugs, proteins and peptides, enantiomers, and anions

Capillary electrophoresis‐mass spectrometry of peptides from enzymatic protein hydrolysis: Simulation and optimization

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