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

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...

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Detalles Bibliográficos
Autores principales: Sharma, Sujata, Sinha, Mau, Kaushik, Sanket, Kaur, Punit, Singh, Tej P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3671519/
https://www.ncbi.nlm.nih.gov/pubmed/23762557
http://dx.doi.org/10.1155/2013/271641
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author Sharma, Sujata
Sinha, Mau
Kaushik, Sanket
Kaur, Punit
Singh, Tej P.
author_facet Sharma, Sujata
Sinha, Mau
Kaushik, Sanket
Kaur, Punit
Singh, Tej P.
author_sort Sharma, Sujata
collection PubMed
description 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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spelling pubmed-36715192013-06-12 C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule Sharma, Sujata Sinha, Mau Kaushik, Sanket Kaur, Punit Singh, Tej P. Biochem Res Int Review Article 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. Hindawi Publishing Corporation 2013 2013-05-15 /pmc/articles/PMC3671519/ /pubmed/23762557 http://dx.doi.org/10.1155/2013/271641 Text en Copyright © 2013 Sujata Sharma et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Sharma, Sujata
Sinha, Mau
Kaushik, Sanket
Kaur, Punit
Singh, Tej P.
C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule
title C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule
title_full C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule
title_fullStr C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule
title_full_unstemmed C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule
title_short C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule
title_sort c-lobe of lactoferrin: the whole story of the half-molecule
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3671519/
https://www.ncbi.nlm.nih.gov/pubmed/23762557
http://dx.doi.org/10.1155/2013/271641
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