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C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule

Journal

BIOCHEMISTRY RESEARCH INTERNATIONAL
Volume 2013, Issue -, Pages -

Publisher

HINDAWI LTD
DOI: 10.1155/2013/271641

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Funding

  1. Department of Biotechnology (DBT), New Delhi
  2. Department of Biotechnology (DBT)
  3. Indian Council of Medical Research (ICMR), New Delhi
  4. Department of Science and Technology (DST), Ministry of Science and Technology, New Delhi

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Lactoferrin is an iron-binding diferric glycoprotein present in most of the exocrine secretions. The major role of lactoferrin, which is found abundantly in colostrum, is antimicrobial action for the defense of mammary gland and the neonates. Lactoferrin consists of two equal halves, designated as N-lobe and C-lobe, each of which contains one iron-binding site. While the N-lobe of lactoferrin has been extensively studied and is known for its enhanced antimicrobial effect, the C-lobe of lactoferrin mediates various therapeutic functions which are still being discovered. The potential of the C-lobe in the treatment of gastropathy, diabetes, and corneal wounds and injuries has been indicated. This review provides the details of the proteolytic preparation of C-lobe, and interspecies comparisons of its sequence and structure, as well as the scope of its therapeutic applications.

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