Preparative polyacrylamide gel electrophoresis has been used to purify the enterotoxin of Clostridium perfringens from Sephadex G-100 extracts. Purified toxin of high specific activity was eluted in 1 to 3 h, depending upon the length of the acrylamide gel used. Recovery of biological activity with this technique ranged from 80 to 90%. The purity and physical characteristics of the toxin were s...

BACKGROUND Alkyl hydroperoxide reductase (AhpC) of Helicobacter pylori is considered as a diagnostic antigen. Therefore, this antigen can be used to detect H. pylori infection by stool immunoassays such as ELISA. The aim of this study was to simplify the AhpC protein purification procedures. METHODS For whole cell protein extraction, the bacterial cells were ruptured by octly-β-D glucopyranos...

Preparat ive electrophoresis may provide a unique method for meeting ever m o r e stringent purity requirements. Prolonged near zero gravity in space may permi t the operation of preparative electrophoresis equipment with 100 t imes greater throughput than i s currently available. Some experiments with Influenza Virus Antigen, Erythropoietin and Antihemophaliac Factor , along with process and e...

By utilizing conventional techniques of pressure ultrafiltration, gel filtration chromatography, diethylaminoethyl cellulose chromatography, and preparative polyacrylamide electrophoresis, the A component of the group D lysin produced by Streptococcus zymogenes has been purified to a state of apparent homogeneity when determined by the techniques of anionic and cationic disc gel electrophoresis...

In the study reported here, non-histamine chromosomal proteins from proliferative and secretory human endometrium, and from undifferentiated endometrial carcinoma have been separated into more than 750 protein components, using a new preparative and highly sensitive analytical method. The following experimental procedure was applied: 1. Dissociation of chromatin under different conditions (vari...

By utilizing conventional techniques of pressure ultrafiltration, gel filtration chromatography, diethylaminoethyl cellulose chromatography, and preparative polyacrylamide electrophoresis, the A component of the group D lysin produced by Streptococcus zymogenes has been purified to a state of apparent homogeneity when determined by the techniques of anionic and cationic disc gel electrophoresis...