Literature DB >> 14642807

FT-IR study of heterologous protein expression in recombinant Escherichia coli strains.

Diletta Ami1, Loredana Bonecchi, Simona Calì, Gaetano Orsini, Giancarlo Tonon, Silvia Maria Doglia.   

Abstract

Two recombinant Escherichia coli strains expressing different levels of an interferon fusion protein as inclusion bodies have been studied by Fourier transform infrared (FT-IR) microspectroscopy. A marker band at 1628 cm(-1) allowed monitoring of the protein expression by direct analysis of cell pellets in a rapid, non-invasive and quantitative way. The results demonstrate that FT-IR microspectroscopy is a technique of potential biotechnological interest for studying inclusion body formation.

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Year:  2003        PMID： 14642807     DOI： 10.1016/j.bbagen.2003.09.008

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  10 in total

1.  Localization of functional polypeptides in bacterial inclusion bodies.

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Journal:  Appl Environ Microbiol       Date:  2006-11-03       Impact factor: 4.792

2.  A new method to image heme-Fe, total Fe, and aggregated protein levels after intracerebral hemorrhage.

Authors:  Mark J Hackett; Mauren DeSouza; Sally Caine; Brian Bewer; Helen Nichol; Phyllis G Paterson; Frederick Colbourne
Journal:  ACS Chem Neurosci       Date:  2015-03-02       Impact factor: 4.418

3.  Characterization of the Conformational Properties of Soluble and Insoluble Proteins by Fourier Transform Infrared Spectroscopy.

Authors:  Diletta Ami; Antonino Natalello
Journal:  Methods Mol Biol       Date:  2022

4.  Why and how protein aggregation has to be studied in vivo.

Authors:  Diletta Ami; Antonino Natalello; Marina Lotti; Silvia Maria Doglia
Journal:  Microb Cell Fact       Date:  2013-02-15       Impact factor: 5.328

5.  Post-production protein stability: trouble beyond the cell factory.

Authors:  Esther Vazquez; José Luis Corchero; Antonio Villaverde
Journal:  Microb Cell Fact       Date:  2011-08-01       Impact factor: 5.328

6.  The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.

Authors:  Nuria González-Montalbán; Elena García-Fruitós; Salvador Ventura; Anna Arís; Antonio Villaverde
Journal:  Microb Cell Fact       Date:  2006-08-07       Impact factor: 5.328

7.  Sequence determinants of protein aggregation: tools to increase protein solubility.

Authors:  Salvador Ventura
Journal:  Microb Cell Fact       Date:  2005-04-22       Impact factor: 5.328

8.  The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli.

Authors:  Gaetano Invernizzi; Francesco A Aprile; Antonino Natalello; Andrea Ghisleni; Amanda Penco; Annalisa Relini; Silvia M Doglia; Paolo Tortora; Maria E Regonesi
Journal:  PLoS One       Date:  2012-12-14       Impact factor: 3.240

9.  TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.

Authors:  Claudia Capitini; Simona Conti; Michele Perni; Francesca Guidi; Roberta Cascella; Angela De Poli; Amanda Penco; Annalisa Relini; Cristina Cecchi; Fabrizio Chiti
Journal:  PLoS One       Date:  2014-01-30       Impact factor: 3.240

10.  Protein aggregation and membrane lipid modifications under lactic acid stress in wild type and OPI1 deleted Saccharomyces cerevisiae strains.

Authors:  Nadia Maria Berterame; Danilo Porro; Diletta Ami; Paola Branduardi
Journal:  Microb Cell Fact       Date:  2016-02-17       Impact factor: 5.328
  10 in total

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