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      Bovine whey proteins – Overview on their main biological properties

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          Whey, a liquid by-product, is widely accepted to contain many valuable constituents. These include especially proteins that possess important nutritional and biological properties – particularly with regard to promotion of health, as well as prevention of diseases and health conditions. Antimicrobial and antiviral actions, immune system stimulation, anticarcinogenic activity and other metabolic features have indeed been associated with such whey proteins, as α-lactalbumin, β-lactoglobulin, lactoferrin, lactoperoxidase, and bovine serum albumin. The most important advances reported to date pertaining to biological properties of whey proteins are reviewed in this communication.

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          Most cited references 140

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          Lactoferrin--a multifunctional protein with antimicrobial properties.

          Lactoferrin is a member of the transferrin family of iron-binding proteins. Numerous functions have been reported and continue to be reported for the protein, some of which are related to its iron-binding properties. Its extensive antimicrobial activities were originally attributed to its ability to sequester essential iron, however, it is now established that it possesses bactericidal activities as a result of a direct interaction between the protein or lactoferrin-derived peptides. This article reviews the antimicrobial activities of lactoferrin and discusses the potential mode of action of lactoferrin-derived cationic peptides against Gram-negative bacteria in the light of recent studies.
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            Nomenclature of Proteins of Cow's Milk: Fifth Revision

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              Initial interaction of herpes simplex virus with cells is binding to heparan sulfate.

               D WuDunn,  Linda Spear (1988)
              We have shown that cell surface heparan sulfate serves as the initial receptor for both serotypes of herpes simplex virus (HSV). We found that virions could bind to heparin, a related glycosaminoglycan, and that heparin blocked virus adsorption. Agents known to bind to cell surface heparan sulfate blocked viral adsorption and infection. Enzymatic digestion of cell surface heparan sulfate but not of dermatan sulfate or chondroitin sulfate concomitantly reduced the binding of virus to the cells and rendered the cells resistant to infection. Although cell surface heparan sulfate was required for infection by HSV types 1 and 2, the two serotypes may bind to heparan sulfate with different affinities or may recognize different structural features of heparan sulfate. Consistent with their broad host ranges, the two HSV serotypes use as primary receptors ubiquitous cell surface components known to participate in interactions with the extracellular matrix and with other cell surfaces.

                Author and article information

                Food Res Int
                Food Res. Int
                Food Research International (Ottawa, Ont.)
                Elsevier Ltd.
                3 August 2007
                December 2007
                3 August 2007
                : 40
                : 10
                : 1197-1211
                Escola Superior de Biotecnologia, Rua Dr. António Bernardino de Almeida, P-4200-072 Porto, Portugal
                Author notes
                [* ]Corresponding author. Tel.: +351 22 5580004; fax: +351 22 5090351. fxmalcata@
                Copyright © 2007 Elsevier Ltd. All rights reserved.

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.


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