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Binding fatty acid

Kennedy, M.W., Allen, J.E., Wright, A.S., McCruden, A.B. and Cooper, A. (1995a) The gpl5/400 polyprotein antigen of Brugia malayi binds fatty acid and retinoids. Molecular and Biochemical Parasitology 71, 41-50. [Pg.335]

Sacchettini, J.C. and Gordon, J.I. (1993) Rat intestinal fatty acid binding protein a model system for analyzing the forces that can bind fatty acids to proteins. Journal of Biological Chemistry 268, 18399—18402. [Pg.336]

The very low solubility of fatty acids poses a problem for their transport within the cell, as it does in the blood. The problem is solved by the presence of the fatty acid binding protein (FABP). It binds fatty acids at the inner surface of... [Pg.133]

The fatty acids could be carried by proteins by a process similar to the way in which serum albumin binds fatty acid in the bloodstream of mammals. Other types of lipid might be formed into complexes analogous to low-density lipoproteins of the type found in animal tissues, where the lipid core of the lipoprotein is surrounded by a hydrophilic cortex made up of protein, phospholipid, and cholesterol (87). This allows the lipid to be moved in an aqueous environment. The protein of the lipoprotein shell could also act as possible ligands for particular receptors at the membrane of the cell at which the export occurs. The lipoproteins, if they are present, would probably be formed within the endomembrane lumen and would receive the proteins at the endoplasmic reticulum. [Pg.14]

The fluidity of the hydrogen-bond donation network at the pore could allow a large number of structurally distinct molecules to bind in this location. If the function of the pocket is to bind fatty acids or other structurally diverse pocket factors and thus stabilize the virion. The flexibility of the hydrogenbonding network at the pore seems ideally suited for such a purpose. [Pg.512]

Lipase is known to catalyze esterification through an acyl-intermediate formed between the fatty acid substrate and the enzyme. Free enzyme can bind fatty acid to produce either this intermediate or the ester product. With a high concentration of alcohol, the acyl-intermediate will be consumed, and the enzyme may then start to bind product and catalyze its hydrolysis, thereby reversing the reaction. When present in an excess of fatty acid, however, most of the enzyme is found in the acylated form, preventing it from binding the product (15,16). [Pg.193]

Lactoglobulin 8.0 3.3 Retinol carrier, binding fatty acids, Perez and Calvo (1995) ... [Pg.178]

Under conditions of low light intensity, the all-trans-retinaldehyde released from rhodopsin is reduced to aU-fra s-retinol, which is then transported to the retinal pigment epithelium bound to the interphotoreceptor RBP. This protein also binds fatty acids, including palmitate and docosa-hexaenoic acid (C22 6 co3), which is known to be essential for vision and which comprises some 50% of the phospholipid of photoreceptor cells. [Pg.52]

In the members of the iLBP family whose function is to bind fatty acids, the cavity does not mirror the shape of the ligand. This should be apparent in Fig. 8. Note that the overall shape is ellipsoidal despite the fact that the protein mainly binds fatty acids and other generally elongated molecules. In CRBP and CRBPII, the cavity has a closer fit to the ligand (Cowan et ai, 1993). Except for MFB2, the bottom of the cavity is close to the center of the molecule and the top is near helix all and turns between /3C and /8D, j8 , and )8F. [Pg.110]

Fig. 14. The recognition motifs in the iLBPs. The amino acids are numbered according to their location in crystalline ALBP, but corresponding amino acids present in the other crystalline proteins are also listed. Two locations for fatty acids can be seen, one where fatty acid is bound to ALBP, P2, MFB2, and HFABP the other where IFABP binds fatty acids. The position of bound retinol in CRBP and CRBPII is also shown, although because the /3-ionone ring is edge-on, it is not readily distinguished from a fatty acid. Note that the polar residues can be either ionizable or polar (Arg or Gin and Tyr). Further details of structural factors in the three motifs are given in the text. Fig. 14. The recognition motifs in the iLBPs. The amino acids are numbered according to their location in crystalline ALBP, but corresponding amino acids present in the other crystalline proteins are also listed. Two locations for fatty acids can be seen, one where fatty acid is bound to ALBP, P2, MFB2, and HFABP the other where IFABP binds fatty acids. The position of bound retinol in CRBP and CRBPII is also shown, although because the /3-ionone ring is edge-on, it is not readily distinguished from a fatty acid. Note that the polar residues can be either ionizable or polar (Arg or Gin and Tyr). Further details of structural factors in the three motifs are given in the text.
El and ET cannot bind fatty acid and thus neither can catalyze the cyclooxygenase reaction. For aspirin, conversion of El to El is accompanied by covalent modification of the protein, making the transition irreversible. [Pg.299]

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. [Pg.424]

Hepatocyte nuclear factor 4 is a transcription factor that constitutively binds fatty acids, Structure 2002, 10, 1225-1234. [Pg.927]

P. falciparum cultivated in vitro incorporates free fatty acids (FFA) into the major PhL species and other complex lipids (42,43). Infected erythrocytes contain significantly higher acyl-CoA synthetase activity than normal erythrocytes (44). Although Plasmodium fatty acid transfer proteins have not been described, the surface of P. falciparum merozoites shows a 75 kDa heat shock protein cognate, which are known to bind fatty acids (2). [Pg.137]

However, several other sites on p-LG have been reported to bind fatty acids. At pH 7, increasing dimer formation as a result of increased concentration has been found to eliminate palmitate binding sites on the monomer, while forming a higher affinity pocket. Fatty acids have also been found to bind to the external site in the groove between the a-helix and the p-barrel. ... [Pg.732]


See other pages where Binding fatty acid is mentioned: [Pg.325]    [Pg.328]    [Pg.746]    [Pg.121]    [Pg.308]    [Pg.530]    [Pg.179]    [Pg.1328]    [Pg.103]    [Pg.122]    [Pg.124]    [Pg.124]    [Pg.130]    [Pg.130]    [Pg.133]    [Pg.335]    [Pg.298]    [Pg.82]    [Pg.273]    [Pg.252]    [Pg.732]    [Pg.255]    [Pg.659]    [Pg.325]    [Pg.177]    [Pg.344]    [Pg.543]   
See also in sourсe #XX -- [ Pg.75 ]




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