Expression and purification of active WW domains of FBP11/HYPA and FBP28/CA150.
Production of GST-fused WW domains of FBP proteins was increased using the bubbling cultivation method for E. coli. Purified WW domains of FBP11 and FBP28 bound a PL motif peptide with dissociation constants (K(D)) of 248 +/- 27 and 1880 +/- 280 microM, respectively.
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. amtanok@mail.ecc.u-tokyo.ac.jp.
Yusuke
Y
Kato
Yoriko
Y
Sawano
Masaru
M
Tanokura
D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression / Q000235:genetics*; D010957:Plasmids / Q000235:genetics; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D020349:Surface Plasmon Resonance; D015534:Trans-Activators / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*
D002352:Carrier Proteins; D011994:Recombinant Proteins; D015534:Trans-Activators