Improved factor Xa cleavage of fusion proteins containing maltose binding protein.
The addition of five glycine residues at a position adjacent to the factor Xa cleavage site of a MBP-2C fusion protein, comprising maltose binding protein (MBP) and poliovirus 2C, allowed factor Xa to generate both of the component proteins. If, however, MBP-2C was without the above modification, it was cleaved only at a site located internally within poliovirus 2C, and this protein was not, therefore, generated by factor Xa cleavage. A simple procedure is described that uses PCR for the introduction of five glycines adjacent to the factor Xa recognition site.
Rodríguez
P L
PL
Centro de Biología Molecular, Universidad Autónoma de Madrid, Spain.
Carrasco
L
L
D000595:Amino Acid Sequence; D001483:Base Sequence; D015153:Blotting, Western; D002352:Carrier Proteins / Q000737:chemistry*; D015951:Factor Xa / Q000737:chemistry*; D005998:Glycine / Q000737:chemistry; D058619:Maltose-Binding Proteins; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry; D010957:Plasmids / Q000737:chemistry; D014760:Viral Fusion Proteins / Q000737:chemistry*; D017361:Viral Nonstructural Proteins / Q000737:chemistry
D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D014760:Viral Fusion Proteins; D017361:Viral Nonstructural Proteins; D010447:Peptide Hydrolases; D015951:Factor Xa; C076023:2C protein, viral; D005998:Glycine