Difference between revisions of "Part:BBa K2924041"
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===References===
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===Functional Parameters===
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<partinfo>References</partinfo>
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1. Legrand, D., Elass, E., Carpentier, M., & Mazurier, J. (2005). Lactoferrin. Cellular and Molecular Life Sciences, 62(22), 2549.
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2.Ward, P. P., Paz, E., & Conneely, O. M. (2005). Lactoferrin. Cellular and Molecular Life Sciences, 62(22), 2540.
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[1]: Ringquist, S., Shinedlind, S., Barrick, D., Green, L., Binkley, J., Stormo, G. D., Gold, L. "Translation initiation in Escherichia coli: sequences within the ribosome‐binding site." <i>Molecular microbiology</i> 6.9 (1992): 1219-1229.
  
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3. Iyer, S., & Lonnerdal, B. (1993). Lactoferrin, lactoferrin receptors and iron metabolism. European journal of clinical nutrition.
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[2]:  Heidorn T., Camsund, D., Huang, H.-H., Lindberg, P., Oliveira, P., Stensjö, K., Lindberg, P. "Synthetic biology in cyanobacteria: engineering and analyzing novel functions." <i>Methods in enzymology.</i> Vol. 497. Academic Press, 2011. 539-579.

Revision as of 15:32, 20 October 2019


Lactoferrin

Lactoferrin is a gene coding for a protein product which originates from Bos taurus.

Lactoferrin is a multifunctional protein from the transferrin group, which is assigned to serine proteases due to its enzymatic activity. In addition, lactoferrin also has nuclease activity and is an iron chelator1 Lactoferrin consists of a polypeptide chain with about 700 amino acids and forms two similar globular domains called N-lobes and C-lobes. The N lobe is formed by amino acid residues 1 to 333, the C lobe by amino acid residues 345 to 692. The two domains are connected by a short alpha helix2. Each flap consists of two subdomains (N1 and N2 as well as C1 and C2) and contains one position each for binding iron and another for glycosylation. The extent of glycosylation can vary, which explains the variation in molecular weight between 76 and 80 kDa. Lactoferrin is a basic protein. Its isoelectric point is at a pH of 8.7. It can reversibly bind two metal ions in its domains, e.g. iron, zinc or copper. The affinity of lactoferrin to iron is about 300 times higher than that of transferrin. A distinction is made between hololactoferrin rich in iron and iron-free apolactoferrin3. The protein lactoferrin reduces inflammation factors and thus promotes the absorption of iron into the blood and its availability in the body.


References

[1]: Ringquist, S., Shinedlind, S., Barrick, D., Green, L., Binkley, J., Stormo, G. D., Gold, L. "Translation initiation in Escherichia coli: sequences within the ribosome‐binding site." Molecular microbiology 6.9 (1992): 1219-1229.

[2]: Heidorn T., Camsund, D., Huang, H.-H., Lindberg, P., Oliveira, P., Stensjö, K., Lindberg, P. "Synthetic biology in cyanobacteria: engineering and analyzing novel functions." Methods in enzymology. Vol. 497. Academic Press, 2011. 539-579.