Fatty acid-binding proteins figure

Acetoacetate and /3-hydroxybutyrate are transported through the blood from liver to target organs and tissues, where they are converted to acetyl-CoA (Figure 24.29). Ketone bodies are easily transportable forms of fatty acids that move through the circulatory system without the need for eomplexation with serum albumin and other fatty acid—binding proteins. 

Figure 13.2 Schematic representation of the creation of hPXR humanized mice. The humanization was achieved in the liver only when the liver-specific albumin promoter was used to direct the transgene expression, or in both the liver and the intestine when the fatty acid binding protein promoter was used. PCN, pregnenolone-16a-carbonitrile RIF, rifampicin. + and mean induction and lack of induction, respectively.

Figure 7.8 Comparison of oxygen transport from lung to a cell and then into a mitochondrion with fatty acid transport from an adipocyte to a cell and then into the mitochondria in various tissues/ organs. Fatty add is transported in blood bound to albumin, oxygen is transported in blood bound to haemoglobin. Fatly add is transported within the cell attached to the fatty acid-binding protein (BP), oxygen is transported within a cell attached to myoglobin (Mb). Alb represents albumin, Hb haemoglobin.

Figure S.6 Derivatization reagents for the preparation of pyridoxamine conjugates of fatty acid binding proteins.

Figure 5.7 Single turnover, reductive animation, reactions promoted by fatty acid binding protein-pyridoxamine conjugates.

In schematic diagrams, P strands are usually depicted by broad arrows pointing in the direction of the carboxyl-terminal end to indicate the type of P sheet formed—parallel or antiparallel. More structurally diverse than a helices, P sheets can be relatively flat but most adopt a somewhat twisted shape (Figure 3.40). The P sheet is an important structural element in many proteins. For example, fatty acid-binding proteins, important for lipid metabolism, are built almost entirely from P sheets (Figure 3.41). 

Figure 3.41. A Protein Rich in p Sheets. The structure of a fatty acid-binding protein. 

Figure 2. Calculated vs. observed free energies of binding for DHFR complexes (circles), the arabinose complex with arabinose binding protein (triangle), the lysine complex with lysine binding protein (diamond), the complexes of stearate and elaidate with muscular fatty acid binding protein (squares) and the complexes of retinol, retinoic acid, n-ethyl-retinamide and fenretinide with bovine plasma RBP (stars).

Unesterified fatty acids within cells are commonly bound by fatty acid-binding proteins (FABPs), which belong to a group of small cytosolic proteins that facilitate the Intracellular movement of many lipids. These proteins contain a hydrophobic pocket lined by p sheets (Figure 18-3). A long-chain fatty acid can fit into this pocket and Interact noncovalently with the surrounding protein. 

A related family of proteins are represented by fatty acid-binding proteins and by the intracellular retinol- and retinoic acid-binding proteins (see also Box 22-A).p These are 10-stranded antiparallel p-barrels with two helices blocking an end (see Figure). 

Figure 36-3 shows several microdialyzers, from 5 well to 96 well and for sample sizes from 20 juL to 60 jxL. They are advertised for desalting macromolecules, changing buffer or pH of sample solutions, purifying viruses after a sucrose gradient, binding fatty acids to proteins, and concentrating antibodies. Because of the small volume, equilibrium is achieved in 1 hour. 

---