An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein-Reference-Cited by-同舟云学术

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An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein

Published:1988-12 Issue:2 Volume:74 Page:365-373
ISSN:0378-1119
Container-title:Gene
language:en
Short-container-title:Gene

Author:

Maina Claude V.,Riggs Paul D.,Grandea Andres G.,Slatko Barton E.,Moran Laurie S.,Tagliamonte John A.,McReynolds Larry A.,Chu di Guan

Publisher

Elsevier BV

Subject

Genetics,General Medicine

Reference24 articles.

1. Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose;Bedouelle;Eur. J. Biochem.,1988

2. In vitro gene fusions that join an enzymatically active β-galactosidase segment to amino-terminal fragments of exogenous proteins: Escherichia coli plasmid vectors for the detection and cloning of translational initiation signals;Casadaban;J. Bacteriol.,1980

3. Paramyosin and the filaments of molluscan ‘catch’ muscles I. Paramyosin: structure and assembly;Cohen;J. Mol. Biol.,1971

4. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein;Guan;Gene,1988

5. Rapid purification of a cloned gene product by genetic fusion and site-specific proteolysis;Germino,1984

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