Expression and purification of active WW domains of FBP11/HYPA and FBP28/CA150

Yusuke Kato; Yoriko Sawano; Masaru Tanokura

doi:10.2174/092986606775101670

Expression and purification of active WW domains of FBP11/HYPA and FBP28/CA150

Protein Pept Lett. 2006;13(2):197-201. doi: 10.2174/092986606775101670.

Authors

Yusuke Kato¹, Yoriko Sawano, Masaru Tanokura

Affiliation

¹ 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.

PMID: 16472085
DOI: 10.2174/092986606775101670

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Carrier Proteins / chemistry*
Carrier Proteins / genetics
Carrier Proteins / isolation & purification*
Escherichia coli / genetics
Escherichia coli / metabolism
Gene Expression / genetics*
Plasmids / genetics
Protein Structure, Tertiary
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / isolation & purification
Surface Plasmon Resonance
Trans-Activators / chemistry*
Trans-Activators / genetics
Trans-Activators / isolation & purification*

Substances

Carrier Proteins
Recombinant Proteins
Trans-Activators