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

最初

Salt Effects on the Physical Properties of the Transferrins,as undertaken to examine the effect of NaCl on the related proteins ovotransferrin and lactoferrin. EPR difference spectroscopy was used to probe changes in the metal site of these proteins. Sodium chloride was found to perturb the g′ = 4.3 EPR spectra of both ovotransferrin and lactoferrin but in d

gentle

Interaction of Lactoferrin with Sequestered Transition Metal Ions,copper, zinc and iron are so reactive that the biochemical reactions dependent on these essential elements typically involve the formation of specific protein-metal ion complexes or chelates. Indeed, the absorption, transport, cellular accumulation, and steady-state molecular distribution of these t

peak-flow

Merited

The Effects of Lactoferrin on Gram-Negative Bacteria,f functions have been ascribed to the protein, and it appears to contribute to antimicrobial host defense. In particular, it has been shown to have direct effects on pathogenic microorganisms including bacteriostasis and the induction of microbial iron uptake systems. Still its overall physiologic r

Anemia

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The Monocytic Receptor for Lactoferrin and its Involvement in Lactoferrin-Mediated Iron Transport,om the monocyte/macrophage family. Among these, an important role of lactoferrin as responsible for the inflammatory-induced blood hyposideremia and accumulation of iron in the monocyte/macrophage system has been suggested mainly based on experiments in rodents..In a series of experiments we have ex

苦惱

Study on the Binding of Lactotransferrin (Lactoferrin) to Human PHA-Activated Lymphocytes and Non-Ao)ethyl-1,3′- dithiopropionate (SASD)* on Lys-74 inhibits the binding of the glycoprotein to both human PHA-activated lymphocytes and non-activated platelets. This suggests that the cell binding site of lactotransferrin is located in the vicinity of the lysine residues 74 & 264 and does not occur ei

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Physical Characteristics and Polymerization During Iron Saturation of Lactoferrin, A Myelopoietic R associated with progression of leukemia and other hematopoietic disorders. LF may be clinically useful and for this reason we studied selected biochemical characteristics of LF. Purified human milk LF was saturated with iron from solution and analyzed by gel electrophoresis, ion-exchange and gel fi

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The Role of Lactoferrin as an Anti-Inflammatory Molecule,ammatory tissue injury. The fact that neutrophils contain lactoferrin and mononuclear phagocytes have the capacity to acquire exogenous iron has suggested that iron bound to lactoferrin may influence the nature of free radical products generated by these cells. Over the years the iron-lactoferrin co