Titlebook: Cellular Lipid Binding Proteins; Jan F. C. Glatz Book 2002 Springer Science+Business Media Dordrecht 2002 DNA.Lipid.biochemistry.gene expr

Lumbar-Stenosis

Ccu106

Similar mechanisms of fatty acid transfer from human anal rodent fatty acid-binding proteins to memase of human IFABP, both the Ala.and Thr. forms were examined. The results show clearly that for all FABPs examined, the mechanisms of ligand transfer observed for rodent proteins hold true for their human counterparts. Moreover, it appears that the Ala to Thr substitution at residue 54 of the human

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Cytosolic fatty acid binding proteins catalyze two distinct steps in intracellular transport of the’ membrane. Membrane-active FABPs catalyze dissociation of the fatty acid from the donor membrane and binding to the acceptor membrane, while membrane-inactive FABPs catalyze diffusion of fatty acids across the aqueous cytosol. Thus, FABPs catalyze all three steps in intracellular transport. A simpl

FOVEA

Insights into binding of fatty acids by fatty acid binding proteins,ty acids. The ADIFAB-method is a fluorescent test for fatty acid in equilibrium with iLBP and reveals some correlation of binding affinity to fatty acid solubility in the aqueous phase; these data are often at variance with those obtained by the other methods. Thus, in this review published binding

Peak-Bone-Mass

健壮

Solution structure of fatty acid-binding protein from human brain,d with docosahexaenoic acid [12] reveals only minor differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP and heart-type FABP with respect to fatty acid binding inside the protein cavity. (Mol Cell Biochem .

Motilin

Evolution of the family of intracellular lipid binding proteins in vertebrates,plasmic trafficking of distinct ligands. It is speculated that recruitment of an iLBP during evolution of animals enabled the mitochondrial oxidation of long-chain fatty acids. (Mol Cell Biochem .: 69–77, 2002)

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Overstate

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