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Titlebook: Lactoferrin; Structure and Functi T. William Hutchens,Sylvia V. Rumball,Bo Lönnerdal Book 1994 The Editor(s) (if applicable) and The Author

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书目名称Lactoferrin
副标题Structure and Functi
编辑T. William Hutchens,Sylvia V. Rumball,Bo Lönnerdal
视频video
丛书名称Advances in Experimental Medicine and Biology
图书封面Titlebook: Lactoferrin; Structure and Functi T. William Hutchens,Sylvia V. Rumball,Bo Lönnerdal Book 1994 The Editor(s) (if applicable) and The Author
描述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-known 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
出版日期Book 1994
关键词bacteria; biology; ferritin; growth; molecular biology; protein; proteins
版次1
doihttps://doi.org/10.1007/978-1-4615-2548-6
isbn_softcover978-1-4613-6087-2
isbn_ebook978-1-4615-2548-6Series ISSN 0065-2598 Series E-ISSN 2214-8019
issn_series 0065-2598
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Busines
The information of publication is updating

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发表于 2025-3-21 23:17:59 | 显示全部楼层
0065-2598 ion on this protein has been too limited and diffuse, partly because it has been "hidden" among other well-known 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 w
发表于 2025-3-22 04:28:30 | 显示全部楼层
Physical Characteristics and Polymerization During Iron Saturation of Lactoferrin, A Myelopoietic R chromatography demonstrated the binding of LF to both anionic and cationic media under identical conditions indicating a bipolar charge distribution. Gel filtration studies revealed a tetramerized form of LF, the formation and stability of which was dependent on the ionic strength of the solution.
发表于 2025-3-22 05:28:50 | 显示全部楼层
Maternal Lactoferrin in the Urine of Preterm Infants,s absorbed intact by the preterm infant and appears to remain structurally and functionally intact within the circulatory system and during urinary excretion. It is possible, therefore, that maternal lactoferrin has an immunoregulatory influence in newborn infants fed human milk.
发表于 2025-3-22 10:54:01 | 显示全部楼层
Interaction of Lactoferrin with Sequestered Transition Metal Ions, protein-metal ion complexes or chelates. Indeed, the absorption, transport, cellular accumulation, and steady-state molecular distribution of these transition metal ions within and between intracellular compartments would appear to be determined, in part, by a series of directional metal ion transfer events between macromolecules.
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