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Related Experiment Video

Updated: Jul 17, 2026

Quantifying Plant Soluble Protein and Digestible Carbohydrate Content, Using Corn (Zea mays) As an Exemplar
07:19

Quantifying Plant Soluble Protein and Digestible Carbohydrate Content, Using Corn (Zea mays) As an Exemplar

Published on: August 6, 2018

A method for three-dimensional protein characterization and its application to a complex plant (corn) extract.

Zhengrong Gu1, Charles E Glatz

  • 1Department of Chemical and Biological Engineering, Iowa State University, Ames, IA 50011-2230, USA.

Biotechnology and Bioengineering
|January 26, 2007
PubMed
Summary

A new method maps host proteins using surface hydrophobicity, isoelectric point, and molecular weight. This aids in selecting hosts and tissues for recombinant protein production and purification.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Biotechnology

Background:

  • Understanding host protein properties is crucial for efficient recombinant protein production and purification.
  • Selecting appropriate expression hosts and tissues requires knowledge of their protein characteristics.
  • Existing methods may not comprehensively capture the multi-dimensional properties of host proteins.

Purpose of the Study:

  • To develop a novel method for creating a three-dimensional (3D) map of host protein properties.
  • To characterize surface hydrophobicity (SH), isoelectric point (pI), and molecular weight (MW) of aqueous soluble proteins.
  • To facilitate host selection and optimize recombinant protein purification strategies.

Main Methods:

  • Utilized hydrophobic partitioning in an aqueous two-phase (ATP) system (PEG 3350-Na(2)SO(4)-NaCl).

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Last Updated: Jul 17, 2026

Quantifying Plant Soluble Protein and Digestible Carbohydrate Content, Using Corn (Zea mays) As an Exemplar
07:19

Quantifying Plant Soluble Protein and Digestible Carbohydrate Content, Using Corn (Zea mays) As an Exemplar

Published on: August 6, 2018

mRNA Interactome Capture from Plant Protoplasts
12:29

mRNA Interactome Capture from Plant Protoplasts

Published on: July 28, 2017

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

  • Employed quantitative 2D-electrophoresis to analyze proteins in different phases and the original extract.
  • Established a correlation between partition coefficients and surface hydrophobicity using model proteins.

    • Main Results:

    • Successfully generated a 3D map of host protein properties (SH, pI, MW).
    • Quantified protein partition coefficients by matching spots across 2D gels.
    • Demonstrated the method's applicability to model protein mixtures and complex biological samples like corn germ proteins.

    Conclusions:

    • The developed method provides a comprehensive characterization of host proteins.
    • This 3D protein mapping aids in optimizing recombinant protein expression and purification processes.
    • The technique is valuable for host-pathogen interaction studies and biotechnological applications.