Expression and Purification of Active WW Domains of FBP11/HYPA and FBP28/CA150

Yusuke      Kato; Yoriko      Sawano; Masaru      Tanokura

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 (KD) of 248 ± 27 and 1880 ± 280 μM, respectively.

Keywords: WW domain, air pump, reverse phase chromatography, surface plasmon resonance

« Previous Next »

Rights & Permissions Print Cite

Protein & Peptide Letters

Title: Expression and Purification of Active WW Domains of FBP11/HYPA and FBP28/CA150

Volume: 13 Issue: 2

Author(s): Yusuke Kato, Yoriko Sawano and Masaru Tanokura

Affiliation:

Keywords: WW domain, air pump, reverse phase chromatography, surface plasmon resonance

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 (KD) of 248 ± 27 and 1880 ± 280 μM, respectively.

Export Options

Export File:

RIS (for EndNote, Reference Manager, ProCite)

BibTeX

Text

Content:

Citation Only

Citation and Abstract

About this article

Cite this article as:

Kato Yusuke, Sawano Yoriko and Tanokura Masaru, Expression and Purification of Active WW Domains of FBP11/HYPA and FBP28/CA150, Protein & Peptide Letters 2006; 13 (2) . https://dx.doi.org/10.2174/092986606775101670