Advertisement

Lactoferrin pp 259-263 | Cite as

Cloning and Expression of the C-Terminal Lobe of Human Lactoferrin

  • Bhavwanti Sheth
  • Kathryn M. Stowell
  • Catherine L. Day
  • Edward N. Baker
  • John W. Tweedie
Part of the Advances in, Experimental Medicine and Biology book series (AEMB, volume 357)

Abstract

Three dimensional studies of human lactoferrin (Anderson et al, 1989) have shown that like all other members of the transferrin family, lactoferrin is divided into two lobes; the N-terminal and the C-terminal lobes. Each lobe is capable of synergistically binding one Fe3+ ion and one anion. The cloning of the cDNA for human lactoferrin (hLf) and its subsequent expression in mammalian cells (Stowell et al, 1991) has provided an excellent system to probe the structure and function of hLf by site-directed mutagenesis. The first mutant to be cloned and expressed using this system was the N-terminal lobe (LfN) of hLf (Day et al, 1992). Recombinant protein concentrations of up to 30 mg/1 in the tissue culture medium have been obtained.

Keywords

Signal Peptide Sequence Signal Peptidase Baby Hamster Kidney Cell Human Lactoferrin Dimensional Study 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Anderson, B.F., Baker, H.M., Norris, G.E., Rice, D.W. and Baker, E.N. (1989) Structure of human lactoferrin: Structure analysis and refinement at 2.8 Å resolution. J. Mol. Biol. 209 711–734PubMedCrossRefGoogle Scholar
  2. Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K. and Tomita, M. (1992). Identification of the bactericidal domain of lactoferrin. Biochimica et Biophysica Acta 1121 130–136PubMedCrossRefGoogle Scholar
  3. Day, C.L., Stowell, K.M., Baker, E.N. and Tweedie, J.W. (1992) Studies of the N terminal half of human lactoferrin produced from the cloned cDNA demonstrate that interlobe interactions modulate iron release. J. Biol. Chem. 267 13857–13862PubMedGoogle Scholar
  4. Stowell, K.M., Rado, T.A. Funk, W.D. and Tweedie, J.W. (1991) Expression of cloned human lactoferrin in baby-hamster kidney cells. Biochem. J. 276 349–355PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Bhavwanti Sheth
    • 1
  • Kathryn M. Stowell
    • 1
  • Catherine L. Day
    • 1
  • Edward N. Baker
    • 1
  • John W. Tweedie
    • 1
  1. 1.Department of Chemistry and BiochemistryMassey UniversityPalmerston NorthNew Zealand

Personalised recommendations