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Expression and purification of human amelogenin mature peptide in Escherichia coli / 中华口腔医学杂志
Chinese Journal of Stomatology ; (12): 279-281, 2009.
Article in Chinese | WPRIM (Western Pacific) | ID: wpr-346748
Responsible library: WPRO
ABSTRACT
<p><b>OBJECTIVE</b>To establish the expression and purification route for human amelogenin mature peptide in Escherichia coli and obtain the purified amelogenin (AMG) mature peptide.</p><p><b>METHODS</b>Recombined plasmid pGEX-4T-1-AMG was transformed to Escherichia coli BL21. After expression, AMG was purified with glutathione S-transferase fusion protein purification system (GSTrapFF) column.</p><p><b>RESULTS</b>Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting hybridization results showed that 45,000 GST-AMG fusing protein and 19,000 target AMG mature peptide were obtained successfully.</p><p><b>CONCLUSIONS</b>pGEX-4T-1-AMG-BL21 system is used successfully to express and purify human AMG mature peptide.</p>
Subject(s)
Full text: Available Health context: Neglected Diseases Health problem: Neglected Diseases / Zoonoses Database: WPRIM (Western Pacific) Main subject: Peptides / Recombinant Fusion Proteins / Recombinant Proteins / Electrophoresis, Polyacrylamide Gel / Escherichia coli / Amelogenin / Genetics / Glutathione Transferase / Metabolism Limits: Humans Language: Chinese Journal: Chinese Journal of Stomatology Year: 2009 Document type: Article
Full text: Available Health context: Neglected Diseases Health problem: Neglected Diseases / Zoonoses Database: WPRIM (Western Pacific) Main subject: Peptides / Recombinant Fusion Proteins / Recombinant Proteins / Electrophoresis, Polyacrylamide Gel / Escherichia coli / Amelogenin / Genetics / Glutathione Transferase / Metabolism Limits: Humans Language: Chinese Journal: Chinese Journal of Stomatology Year: 2009 Document type: Article
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