CE in Biotechnology: Practical Applications for Protein and by Anthony B. Chen, Wassim Nashabeh, Timothy Wehr, Kevin D.

By Anthony B. Chen, Wassim Nashabeh, Timothy Wehr, Kevin D. Altria

The carrying on with improvement of capillary electrophoresis (CE) is obvious via the expanding variety of magazine articles, textual content books and symposia dedicated to CE. This monograph is a part of a continuous sequence masking person parts of CE.

The Symposium 'CE in Biotechnology: functional functions for Protein research' was once held in San Francisco, California, united states on August 18, 1999. The symposium highlighted useful purposes, together with tools which had bought regulatory acclaim for the regimen research of advertised recombinant protein prescription drugs. This assembly validated that CE has stumbled on a distinct segment within the regimen research of proteins and peptides in an business environment. The editors of this monograph, besides the sequence editor (Kevin Altria) have been of the opinion that the complaints of that assembly may supply the foundation for theoretical and sensible concerns with regards to the research of healing proteins and peptides by way of CE. This book accordingly involves a number of the useful purposes that have been offered by way of scientists from major biotechnology businesses. numerous entire overview chapters, together with 'CE within the improvement of recombinant protein biopharmaceuticals', 'Selection of buffers in CZE: software to peptide and protein research' and 'Recent advances in cIEF' are incorporated as supplemental information.

This book may be learn by means of these trying to improve and/or validate tips on how to be used for regimen research of proteins and peptides for drug improvement and qc.

Show description

Read Online or Download CE in Biotechnology: Practical Applications for Protein and Peptide Analyses PDF

Similar nonfiction_7 books

Collaborative Virtual Environments: Digital Places and Spaces for Interaction

Collaborative digital Environments (CVEs) are on-line electronic areas and areas the place we will be in contact, play jointly and interact, even if we're, geographically talking, worlds aside. we will hang around, current substitute selves, engage with sensible and terrific items and perform very unlikely manoeuvres.

Dissociative Recombination of Molecular Ions with Electrons

Dissociative Recombination of Molecular Ions with Electrons is a entire choice of refereed papers describing the newest advancements in dissociative recombination study. The papers are written through the best researchers within the box. the themes coated contain using microwave afterglows, merged beams and garage jewelry to degree expense coefficients and to spot the goods and their yields.

Extra info for CE in Biotechnology: Practical Applications for Protein and Peptide Analyses

Sample text

Smet, M. Trends Anal. Chem. 11,27. ; Hailey. ; Portsmouth. J. 1. Chl'ol11alogr. 1993. 641,147. [8] Sadana,A. Chon. 1992,92,1799. [9] Rickard. : Strohl. G. Anal. Biochem. 1991, 197,197. J. Chl'omatogl'. 1991. 547,544. [II] McLaughlin, Beckman Technical In/()rI1Jation Bulletin. TIBC-l 061991. ; Richards, R. Production, characterization and biological effects of recomb in ani DNA derived human 1FN-y. and 1FN-y analogs, In: De Mayeyer. ; Schellekens, H. eds. The Biology of the 1nlel/el'on System 1983.

A CZE Separation of Analog Group 3. b HPLC Separation of Analog Group 3. 1 amide a! •. 5 11 Migration Time (min) ,. 20 22 3D Retention Time (min) Figure 4. a CZE Separation of Analog Group 4. b HPLC Separation of Analog Group 4. Chromatographia Supplement Vol. 15 ~ i ~ ii! 05 ~! = ! II • ••• ! •• . -. ~ • , a:.. 5 Relative Retention Time N i' . exhibited shorter retention times (Figure 7b). The substitutions resulted in decreased hydrophobicity due to the amphiphilic structure of protegrins. The hydrophobic surface of the protegrin molecule interacts with the hydrophobic RP-HPLC stationary phase.

8 References 30 25 r 20 E c a 15 ~ ::J « 10 undigested starting material E 5 PNGase F digested material 0 -5 0 10 20 30 40 50 60 Time (min) Figure 6. CZE of native and deglycosylated rhDNase. 0. The deglycosylated rhDNase was digested with PNGase F. glycoprotein. Additionally, the enzymatic reaction that releases the asparaginelinked oligosaccharide structures converts these asparagine residues into aspartic acid, adding two negative charges. Finally, the loss of glycosylation structures could expose previously shielded charged surface sites to the surrounding electrical field, altering the electrophoretic mobility of the deglycosylated form.

Download PDF sample

Rated 4.65 of 5 – based on 5 votes