Two-step method to isolate target recombinant protein from co-purified bacterial contaminant SlyD after immobilised metal affinity chromatography-Reference-Cited by-同舟云学术

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Two-step method to isolate target recombinant protein from co-purified bacterial contaminant SlyD after immobilised metal affinity chromatography

Published:2007-06 Issue:1-2 Volume:853 Page:314-319
ISSN:1570-0232
Container-title:Journal of Chromatography B
language:en
Short-container-title:Journal of Chromatography B

Author:

Parsy Céline B.,Chapman Caroline J.,Barnes Antony C.,Robertson John F.,Murray Andrea

Publisher

Elsevier BV

Subject

Cell Biology,Clinical Biochemistry,Biochemistry,General Medicine,Analytical Chemistry

Reference19 articles.

1. Purification of his-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies

2. Reversible Immunoprecipitation Using Histidine- or Glutathione S-Transferase-Tagged Staphylococcal Protein A

3. Design of Angiotensin II Derivatives Suitable for Indirect Affinity Techniques: Potential Applications to Receptor Studies

4. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues

5. Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins.

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3. An Orthogonal Fusion Tag for Efficient Protein Purification;Methods in Molecular Biology;2020-11-01

4. Bacillus subtilis MraY in detergent-free system of nanodiscs wrapped by styrene-maleic acid copolymers;PLOS ONE;2018-11-05

5. SlyD-deficient Escherichia coli strains: A highway to contaminant-free protein extraction;Biochemical and Biophysical Research Communications;2018-05

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