Production of Intact Recombinant Lectins in Escherichia coli

  • J. Hirabayashi
  • Y. Sakakura
  • K. Kasai
Part of the Springer Laboratory book series (SLM)


Production of recombinant proteins in bacterial cells may be the most promising approach when biological constraints limit the quantity of target proteins from natural sources. They can also be expressed in eukaryote cells, if appropriate conditions are fulfilled. However, the prokaryote systems represented by an Escherichia coli system have many practical advantages: (1) facility of cell culture (less time-consuming and more economical), (2) a well-established expression mechanism (easily controllable and reproducible), and (3) high productivity (even a gram-order preparation is possible). On the other hand, eukaryote expression systems are useful when some post-translational modifications (e.g., N-terminal acylation, glycosylation, phosphorylation) are important. Bacterial systems are devoid of such modification machineries. However, the great facility of the E. coli system should be the first choice for an attempt to produce recombinant protein.


Initiation Codon Lectin Gene Mutagenic Oligonucleotide Fusion Form Recombinant Lectin 
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© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • J. Hirabayashi
  • Y. Sakakura
  • K. Kasai

There are no affiliations available

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