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https://hdl.handle.net/2440/794
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Type: | Journal article |
Title: | Physicochemical characteristics of LR3-IGF1 protein inclusion bodies: Electrophoretic mobility studies |
Author: | WangsaWirawan, N. O'Neill, B. Middelberg, A. |
Citation: | Biotechnology Progress, 2001; 17(4):786-790 |
Publisher: | Amer Chemical Soc |
Issue Date: | 2001 |
ISSN: | 8756-7938 1520-6033 |
Statement of Responsibility: | Norbert D. Wangsa-Wirawan, Brian K. O'Neill, and Anton P. J. Middelberg |
Abstract: | A knowledge of the physicochemical properties of inclusion bodies is important for the rational design of potential recovery processes such as flotation and precipitation. In this study, measurement of the size and electrophoretic mobility of protein inclusion bodies and cell debris was undertaken. SDS-PAGE analysis of protein inclusion bodies subjected to different cleaning regimes suggested that electrophoretic mobility provides a qualitative measure of protein inclusion body purity. Electrophoretic mobility as a function of electrolyte type and ionic strength was investigated. The presence of divalent ions produced a stronger effect on electrophoretic mobility compared with monovalent ions. The isoelectric point of cell debris was significantly lower than that for the inclusion bodies. Hence, the contaminating cell debris may be separated from inclusion bodies using flotation by exploiting this difference in isoelectric points. Separation by this method is simple, convenient, and a possible alternative to the conventional route of centrifugation. |
Keywords: | Inclusion Bodies Insulin-Like Growth Factor I Electrophoresis, Polyacrylamide Gel Isoelectric Point Osmolar Concentration |
Description: | Copyright © 2001 American Chemical Society and American Institute of Chemical Engineers |
DOI: | 10.1021/bp010058x |
Published version: | http://pubs.acs.org/cgi-bin/article.cgi/bipret/2001/17/i04/pdf/bp010058x.pdf |
Appears in Collections: | Aurora harvest 6 Chemical Engineering publications |
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