Analysis Of Amino Acid Sequences

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Publisher: Elsevier
ISBN: 008049336X
Size: 77.23 MB
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Analysis Of Amino Acid Sequences by

Original Title: Analysis Of Amino Acid Sequences

Amino acid sequence analysis is useful for the study of problems ranging from modifications of single molecules to complex networks and interactions of species. Many available amino acid sequences are providing the basis for various studies at the proteome level. The dynamics of protein expression and the simulation of complex biological systems in which proteins interact with certain kinetics and in their respective compartments are just about to be tackled. Amino acid sequences will be crucial reference points for such studies. Mass spectrometric analysis of proteins Protein sequence databases Amino acid substitution matrices Amino acid-based phylogeny and alignment Individual variation in protein-coding sequences of the human genome Identifying nature's protein Lego® set

Amino Acid Sequence Analysis And Structural Characterization Of Asparaginase And Pegylated Asparaginase

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Author: Hanwei Zhao
Publisher: Proquest, UMI Dissertation Publishing
ISBN: 9781243402714
Size: 46.15 MB
Format: PDF, Kindle
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Amino Acid Sequence Analysis And Structural Characterization Of Asparaginase And Pegylated Asparaginase by Hanwei Zhao

Original Title: Amino Acid Sequence Analysis And Structural Characterization Of Asparaginase And Pegylated Asparaginase

A biotech company is currently developing a "biosimilar" asparaginase product. In order to support the development, initial characterization has been performed on commercially available Elspar (asparaginase) and Oncaspar (pegylated asparaginase). The amino acid sequence of El spar and Oncaspar were determined by tryptic peptide map/mass spectrometry. For Oncaspar, pegylation of amine groups throughout the polypeptide chain altered the tryptic digestion pattern and peptide recovery on the map. Mass analysis of unpegylated peptides recovered in the map indicated that the amino acid sequence of Oncaspar was identical to that of Elspar. Asparaginase is a homotetramer linked by non-covalent interactions; the subunit mass resolved on C4 reversed phase (RP) - HPLC was obtained through on-line mass spectrometry (MS) and matched the sequence derived from peptide mapping/MS. The sulfhydryl content of both Elspar and Oncaspar was measured using Ellman's assay; the levels of unpaired cysteines were negligible for both samples. The subunit mass of Elspar indicated the presence of one disulfide bond in each subunit, and non-reduced peptide mapping of both Elspar and Oncaspar confirmed a disulfide bond between Cys77 and Cys 105. The heterogeneity in pegylation levels and loci, as well as, the PEG mass disparity itself, made intact mass measurement and assignment of pegylated peptides impossible. Through size exclusion chromatography coupled with on-line multi-angle laser light scattering (SEC-MALLS), the average molar mass of Oncaspar was estimated to be 280 kDa, indicating that the average degree of pegylation was approximately 28 PEGs per asparaginase homotetramer. An asparaginase sample from the company was subjected to primary structural analysis. Amino acid differences at three positions were observed in comparison to Elspar.

Protein Sequencing Protocols

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Author: Bryan John Smith
Publisher: Springer Science & Business Media
ISBN: 1592593429
Size: 40.39 MB
Format: PDF, Mobi
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Protein Sequencing Protocols by Bryan John Smith

Original Title: Protein Sequencing Protocols

Featuring new and updated techniques for determining the sequence of proteins and peptides, this edition includes not only novel approaches to the validation of quality assurance methods, reflecting the current importance of biopharmaceuticals, but also offers a guide to analysis of protein sequence information via the powerful new tools of bioinformatics. Comprehensive and up-to-date, Protein Sequencing Protocols, Second Edition, provides for both novice and expert investigators alike a ready source of easy-to-follow protocols that simplify choosing the most appropriate method for protein sequence determination.

New Methods Of Automated Analysis Of Protein Structures

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Author: J. Daniel Lynn
Publisher: Ardent Media
ISBN: 9780842270991
Size: 41.97 MB
Format: PDF, Docs
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New Methods Of Automated Analysis Of Protein Structures by J. Daniel Lynn

Original Title: New Methods Of Automated Analysis Of Protein Structures

A noncommercial protein sequencing instrument. Analysis of amino acid phenylthiohydantoins by gas chromatography. Advances in the gas chromatographic analysis of amino acid phenyl- and methyl-thiolhydantoins. Gas-liquid chromatography (GLC) of amino acid derivatives. Quantitative procedures for use with the Edman-Begg sequenator: partial sequences of two unusual immunoglobulin light chains, Rzf and Sac...

Techniques In Protein Modification

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Author: Roger L. Lundblad
Publisher: CRC Press
ISBN: 9780849326066
Size: 23.26 MB
Format: PDF
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Techniques In Protein Modification by Roger L. Lundblad

Original Title: Techniques In Protein Modification

This exciting laboratory support book encompasses the encyclopedic coverage of the most frequently used methods for the site-specific chemical modification of proteins. In a concise manner, it presents methods for the characterization of modified proteins, including: amino acid analysis protein sequence analysis chemical cleavage of protein chains chromatographic separation of peptides It also discusses various approaches to the determination of solution protein concentration. It includes a complete literature survey of the various reagents, a list of the most commonly used reagents with their physical and chemical properties, and a list of preferred reagent suppliers.

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