Abstract
Lactoferrin (Lf), an iron binding glycoprotein found in the external secretions and neutrophilic leucocytes of mammals, is thought to be responsible for primary defence against microbial infection, mainly as a result of lactoferrin sequestration of iron required for microbial growth (Weinberg, 1978). Many other functions have been attributed to lactoferrin, including immunomodulation and cell growth regulation (Lönnerdal & Iyer, 1995). The lactoferrin has molecular mass of 80 kDa. The protein folds into two globular lobes, the N-lobe comprising the N-terminal half of the polypeptide chain and C-lobe comprising the C-terminal half of the polypeptide chain. The lobes are connected by a 310-helical 10–12 residue peptide. Each lobe is further subdivided into two domains. Each domain contains a single iron binding site, located in the interdomain cleft.
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Sharma, A.K., Karthikeyan, S., Sharma, S., Yadav, S., Srinivasan, A., Singh, T.P. (1998). Structures of Buffalo and Mare Lactoferrins. In: Spik, G., Legrand, D., Mazurier, J., Pierce, A., Perraudin, JP. (eds) Advances in Lactoferrin Research. Advances in Experimental Medicine and Biology, vol 443. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9068-9_2
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DOI: https://doi.org/10.1007/978-1-4757-9068-9_2
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