Lactoferrin Structure Function (11 results)
- Hardcover
Seller: Books on the Web, Winnipeg, MB, CanadaBooks on the Web
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As new! Hard bound in laminated boards, smaller quarto, volume 357 of Advances in Experimental Medicine and Biology. Xi + Pp298. Includes index. Top corners lightly bumped else a new, unread copy. 760 grams.
Lactoferrin: Structure and Function (Advances in Experimental Medicine and Biology)
Hutchens, T. William (Editor) / Lönnerdal, Bo (Editor) / Rumball, Sylvia V. (Editor)
- Softcover
Seller: Revaluation Books, Exeter, United KingdomRevaluation Books
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Paperback. Condition: Brand New. reprint edition. 309 pages. 9.60x6.10x0.90 inches. In Stock.
Lactoferrin : Structure and Function
Hutchens, T. William (EDT); Rumball, Sylvia V. (EDT); Lonnerdal, Bo (EDT)
- Hardcover
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Lactoferrin : Structure and Function
Hutchens, T. William (EDT); Rumball, Sylvia V. (EDT); Lonnerdal, Bo (EDT)
- Hardcover
Seller: GreatBookPrices, Columbia, MD, U.S.A.GreatBookPrices
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Lactoferrin : Structure and Function
Hutchens, T. William (EDT); Rumball, Sylvia V. (EDT); Lonnerdal, Bo (EDT)
- Hardcover
Seller: GreatBookPricesUK, Woodford Green, United KingdomGreatBookPricesUK
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- Softcover
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Taschenbuch. Condition: Neu. Lactoferrin | Structure and Function | T. William Hutchens (u. a.) | Taschenbuch | xi | Englisch | 2012 | Springer | EAN 9781461360872 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu.
Lactoferrin : Structure and Function
Hutchens, T. William (EDT); Rumball, Sylvia V. (EDT); Lonnerdal, Bo (EDT)
- Hardcover
Seller: GreatBookPricesUK, Woodford Green, United KingdomGreatBookPricesUK
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- Softcover
Seller: AHA-BUCH GmbH, Einbeck, GermanyAHA-BUCH GmbH
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Taschenbuch. Condition: Neu. Druck auf Anfrage Neuware - Printed after ordering - Lactoferrin is an intriguing protein with an interesting structure and several known or suggested biological activities. We feel that attention on this protein has been too limited and diffuse, partly because it has been 'hidden' among other well-k…nown iron-binding proteins such as hemoglobin, ferritin and transferrin, but also perhaps because its biological functions are so diverse. Investigators that focus on lactoferrin represent a wide variety of medical and scientific disciplines that do not usually come together. It was our intention to improve that situation with this symposium. In this book, experts from a variety of disciplines describe the present knowledge of the structural features of lactoferrin, its carbohydrate side chains and its capacity to bind different metal ions and anions. Several of the possible physiological functions of lactoferrin are described in detail, including the role of lactoferrin in bacterial killing, its involvement in growth and proliferation, in immune function and in iron absorption. Aspects of the molecular biology of lactoferrin and its specific interactions with different cell types are also included. Finally, as lactoferrin now has become commercially available in larger quantities, possible industrial applications are discussed. The book should give the interested reader a thorough insight into our present knowledge of lactoferrin.
- Softcover
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Paperback. Condition: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.
- Hardcover
Seller: moluna, Greven, Germanymoluna
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Gebunden. Condition: New.
- Hardcover
Seller: AHA-BUCH GmbH, Einbeck, GermanyAHA-BUCH GmbH
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Buch. Condition: Neu. Neuware - Three-Dimensional Structure of Lactoferrin in Various Functional States.- Characterization of Two Kinds of Lactotransferrin (Lactoferrin) Receptors on Different Target Cells.- Primary and Three-Dimensional Structure of Lactotransferrin (Lactoferrin) Glycans.- Synergism and Substitution in the Lact…oferrins.- Salt Effects on the Physical Properties of the Transferrins.- Interaction of Lactoferrin with Sequestered Transition Metal Ions.- Bactericidal Activity of Different Forms of Lactoferrin.- The Effects of Lactoferrin on Gram-Negative Bacteria.- Faecal Flora in the Newborn: Effect of Lactoferrin and Related Nutrients.- The Monocytic Receptor for Lactoferrin and Its Involvement in Lactoferrin-Mediated Iron Transport.- Study on the Binding of Lactotransferrin (Lactoferrin) to Human PHA-Activated Lymphocytes and Non-Activated Platelets: Localisation and Description of the Receptor-Binding Site.- Physical Characteristics and Polymerization during Iron Saturation of Lactoferrin, a Myelopoietic Regulatory Molecule with Suppressor Activity.- Lactoferrin and the Inflammatory Response.- The Role of Lactoferrin as an Anti-inflammatory Molecule.- Interaction of Lactoferrin with Mononuclear and Colon Carcinoma Cells.- Lactoferrin Receptors in Intestinal Brush Border Membranes.- Maternal Lactoferrin in the Urine of Preterm Infants: Evidence for Retention of Structure and function.- Lactoferrin Gene Promoter in Human and Mouse: Analogous and Dissimilar Characteristics.- Lactoferrin cDNA: Expression and In Vitro Mutagenesis.- Antimicrobial Peptides of Lactoferrin.- Physicochemical and Antibacterial Properties of Lactoferrin and Its Hydrolysate Produced by Heat Treatment at Acidic pH.- A Comparison of the Three-Dimensional Structures of Human Lactoferrin in Its Iron Free and Iron Saturated Forms.- Bovine Lactoferrin: Isolation and Characterisation of Genomic Regulatory Sequences.- X-Ray Structural Analysis of Bovine Lactoferrin at 2.5 Å Resolution.- Binding of Porcine Milk Lactoferrin to Piglet Intestinal Lactoferrin Receptor.- Lactoferrin-Receptor Interaction: Effect of Surface Exposed Histidine Residues.- Kinetic Parameters for the Heat Denaturation of Bovine Lactoferrin in Milk, and Its Effect on Interaction with Monocytes.- Cloning and Expression of the C-Terminal Lobe of Human Lactoferrin.- Crystallographic Studies on Metal and Anion Substituted Human Lactoferrin.- Proposed Mechanisms for the Involvement of Lactoferrin in the Hydrolysis of Nucleic Acids.- Lactoferrin Promotes Nerve Growth Factor Synthesis/Secretion in Mouse Fibroblast L-M Cells.- Summary Chapter: Lactoferrin Structure and Function: Remaining Questions, Methodological Considerations and Future Directions.
