Literature DB >> 8672288

Efficient production from Aspergillus niger of a heterologous protein and an individual protein domain, heavy isotope-labelled, for structure-function analysis.

D A MacKenzie1, J A Spencer, M F Le Gal-Coëffet, D B Archer.   

Abstract

Aspergillus niger has been used successfully to secrete proteins labelled with 13C and/or 15N to a specific activity of > 99% for high resolution NMR analysis. In the case of a heterologous protein, hen egg-white lysozyme, 15N single-labelled and 13C, 15N double-labelled forms were secreted at yields of 100-200 mg l-1 by optimising the type of carbon source used and the ratio of carbon to nitrogen. Another protein, the glucoamylase starch-binding domain from A. niger, was also produced as the 15N single-labelled form at 20-40 mg l-1.

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Year:  1996        PMID: 8672288     DOI: 10.1016/0168-1656(95)00179-4

Source DB:  PubMed          Journal:  J Biotechnol        ISSN: 0168-1656            Impact factor:   3.307


  3 in total

1.  A refined solution structure of hen lysozyme determined using residual dipolar coupling data.

Authors:  H Schwalbe; S B Grimshaw; A Spencer; M Buck; J Boyd; C M Dobson; C Redfield; L J Smith
Journal:  Protein Sci       Date:  2001-04       Impact factor: 6.725

2.  Asparagine and glutamine side-chain conformation in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplings.

Authors:  Victoria A Higman; Jonathan Boyd; Lorna J Smith; Christina Redfield
Journal:  J Biomol NMR       Date:  2004-11       Impact factor: 2.835

3.  Heterologous expression of hen egg white lysozyme and resonance assignment of tryptophan side chains in its non-native states.

Authors:  Christian Schlörb; Katrin Ackermann; Christian Richter; Julia Wirmer; Harald Schwalbe
Journal:  J Biomol NMR       Date:  2005-10       Impact factor: 2.835

  3 in total

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