[2] Analytical peptide mapping of recombinant DNA-derived proteins by reversed-phase high-performance liquid chromatography

Hoff, Edward R.; Chloupek, Rosanne C.

doi:10.1016/s0076-6879(96)71004-2

Cited by 22 publications

(10 citation statements)

References 14 publications

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“…One of the powerful tools of proteome study is obtaining peptide maps via protein digestion followed by MS identification and data processing. Initially, protein digestion was performed by in‐solution approach , which is time consuming, tedious, and inconvenient for automation. Nowadays, it is obvious that these drawbacks can be easily overcome by the application of immobilized enzymes.…”

Section: Application Of Flow‐through Monolithic Bioreactorsmentioning

confidence: 99%

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Влах

Tennikova

2013

J of Separation Science

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In the last decade, the application of monolithic materials has rapidly expanded to the realization of flow-through bioconversion processes. Up to these days, different classes of enzymes such as hydrolases, lyases, and oxidoreductases have been immobilized on organic, inorganic, or hybrid monolithic materials to prepare the effective flow-through enzymes reactors for application in proteomics, biotechnology, pharmaceutics, organic synthesis, and biosensoring. Current review describes the results of kinetic study and specialties of flow-through immobilized enzyme reactors based on the existing monolithic materials.

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Section: Application Of Flow‐through Monolithic Bioreactorsmentioning

confidence: 99%

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Влах

Tennikova

2013

J of Separation Science

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“…Traditionally, because of the reactivity of free sulfhydryl groups, alkylating reagents such as iodoacetic acid or 4-vinyl pyridine have been extensively used to protect free cysteine residues to prevent oxidation or thiol-disulfide exchange (3,4). However, these reagents require basic pH (õpH 8.0) for optimal reactivity at which thiol-disulfide exchange apparently proceeds on the same time scale as alkylation (5).…”

Section: Introductionmentioning

confidence: 99%

Optimization and Applications of CDAP Labeling for the Assignment of Cysteines

et al. 2005

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CDAP is a unique cysteine-labeling reagent because it is reactive under acidic conditions. This provides an advantage over other sulfhydryl labeling reagents as it avoids potential thiol-disulfide exchange. Optimization of the cyanylation reaction allowed the utilization of CDAP as a thiol-directed probe to investigate accessibility of sulfhydryl groups in proteins under various formulation conditions to monitor structural heterogeneity.

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“…Peptide maps are powerful tools for the identification and characterization of proteins and their modifications 1, 2. The sensitivity of a peptide map to small changes in the primary structure of a protein makes it valuable for establishing the identity, purity, and composition of a protein.…”

mentioning

confidence: 99%

“…Peptide maps are powerful tools for the identification and characterization of proteins and their modifications. 1,2 The sensitivity of a peptide map to small changes in the primary structure of a protein makes it valuable for establishing the identity, purity, and composition of a protein. The biopharmaceutical industry, in particular, has used these capabilities to make peptide maps a standard tool for identification and characterization of protein pharmaceuticals.…”

mentioning

confidence: 99%

Use of an integrated MS – multiplexed MS/MS data acquisition strategy for high‐coverage peptide mapping studies

Chakraborty

Berger

Gebler

2007

Rapid Comm Mass Spectrometry

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Liquid chromatography/mass spectrometry (LC/MS) peptide maps have become a basic tool for characterizing proteins of biological and pharmaceutical interest. The ability to generate reproducible maps with high protein sequence coverage is a central goal of methods development. We have applied a recently developed analytical approach (termed LC/MS(E)) to LC/MS peptide mapping. Using the LC/MS(E) approach, the mass detector alternates between a low-energy scanning mode (MS) for accurate mass peptide precursor identification, and an elevated-energy mode (MS(E)) for generation of accurate mass multiplex peptide fragmentation data. In this paper, we evaluate this analytical approach against a tryptic digest of yeast enolase. From the low-energy data, high peptide map coverage (98% of sequence from peptides >3 amino acids) was reproducibly obtained. The MS signal for essentially equimolar peptides varied over 2 orders of magnitude in intensity, and peptide intensities could be precisely and reproducibly measured. Using the temporal constraint that MS(E) peptide fragment ions exhibit chromatographic profiles that parallel the precursor ions that generated them, we were able to produce accurate mass time-resolved MS/MS information for all enolase peptides with sufficient abundance to produce a detectable fragment ion.

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[2] Analytical peptide mapping of recombinant DNA-derived proteins by reversed-phase high-performance liquid chromatography

Cited by 22 publications

References 14 publications

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Optimization and Applications of CDAP Labeling for the Assignment of Cysteines

Use of an integrated MS – multiplexed MS/MS data acquisition strategy for high‐coverage peptide mapping studies

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