[Expression and purification of human amelogenin mature peptide in Escherichia coli].
OBJECTIVE
To establish the expression and purification route for human amelogenin mature peptide in Escherichia coli and obtain the purified amelogenin (AMG) mature peptide.


METHODS
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.


RESULTS
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.


CONCLUSIONS
pGEX-4T-1-AMG-BL21 system is used successfully to express and purify human AMG mature peptide.
Zhang
Xue-Yang
XY
Department of Periodontology, Guangdong Provincial Stomatological Hospital, Guangzhou 510280, China.
Zhang
Jin-Cai
JC
Zhao
Hua
H
D053523:Amelogenin / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D005982:Glutathione Transferase / Q000235:genetics / Q000302:isolation & purification; D006801:Humans; D010455:Peptides / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism
D053523:Amelogenin; D010455:Peptides; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D005982:Glutathione Transferase