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Carotenoid-membrane interactions

Wisniewska, A., J. Widomska, and W. K. Subczynski. 2006. Carotenoid-membrane interactions in liposomes Effect of dipolar, monopolar, and nonpolar carotenoids. Acta Biochim. Polonica 53 475 184. [Pg.212]

McNulty, H.P., J. Byun, S.F. Lockwood, R.F. Jacob, and R.R Mason. 2007. Differential effects of carotenoids on lipid peroxidation due to membrane interactions X-ray diffraction analysis. Biochim. Biophys. Acta 1768 167-174. [Pg.29]

Infrared and Resonance Raman Spectroscopy. Reviewson the uses of resonance Raman spectroscopy in biochemistry and biology include sections on carotenoproteins, visual pigments, and bacteriorhodopsin. The resonance Raman spectrum of the lowest excited triplet state of /3-carotene has been reported.A resonance Raman method has been used for the quantitative analysis of /3-carotene and lutein (20) in tobacco.The mechanism of carotenoid-protein interactions in the carotenoproteins ovoverdin and /3-crustacyanin has been investigated by resonance Raman spectroscopy. " 2 axanthin (24) has been used as a resonance Raman probe of membrane structure. " The resonance Raman spectra have been reported of all-frans-anhydrovitamin A (194), " /3-ionone, retinals, and Schiff bases.The technique has been used extensively to study... [Pg.186]

McMaster, L.D., Kokott, S.A., Reid, S.J., and Abratt, V. 2005. Use of traditional African fermented beverages as delivery vehicles for Bifidobacterium lactis DSM 10140. Int. J. Food Microbiol. 102 231-237. McNulty, H.P., Byun, J., Lockwood, S.F., Jacob, R.F., and Mason, R.P. 2007. Differential effects of carotenoids on lipid peroxidation due to membrane interactions X-ray diffraction analysis. Biochim. Biophys. Acta... [Pg.681]

Little is known of how the biosynthetic metabolon is assembled, what mechanisms control the membrane-specific targeting, and how the conversions to apocarotenoids occur. Yet the current approach to drive import of bacterial or plant genes is to use transit sequences of a stromal protein that may limit the effectiveness of the transgene. In addition, for specific applications of controlling carotenoid composition, we need to better understand the interactions of the various enzymes,... [Pg.383]

NPQ (Rakhimberdieva et al. 2004) exactly matches the absorption spectrum of the carotenoid, 3 -hydrox yech i nenone (Polivka et al. 2005) in the OCP. The OCP is now known to be specifically involved in the phycobilisome-associated NPQ and not in other mechanisms affecting the levels of fluorescence such as state transitions or D1 damage (Wilson et al. 2006). Studies by immunogold labeling and electron microscopy showed that most of the OCP is present in the interthylakoid cytoplasmic region, on the phycobilisome side of the membrane, Figure 1.2 (Wilson et al. 2006). The existence of an interaction between the OCP and the phycobilisomes and thylakoids was supported by the co-isolation of the OCP with the phycobilisome-associated membrane fraction (Wilson et al. 2006, 2007). [Pg.6]

Spin trapping methods were also used to show that when carotenoid-P-cyclodextrin 1 1 inclusion complex is formed (Polyakov et al. 2004), cyclodextrin does not prevent the reaction of carotenoids with Fe3+ ions but does reduce their scavenging rate toward OOH radicals. This implies that different sites of the carotenoid interact with free radicals and the Fe3+ ions. Presumably, the OOH radical attacks only the cyclohexene ring of the carotenoid. This indicates that the torus-shaped cyclodextrins, Scheme 9.6, protects the incorporated carotenoids from reactive oxygen species. Since cyclodextrins are widely used as carriers and stabilizers of dietary carotenoids, this demonstrates a mechanism for their safe delivery to the cell membrane before reaction with oxygen species occurs. [Pg.167]

McNulty, H., R. F. Jacob et al. (2008). Biologic activity of carotenoids related to distinct membrane physicochemical interactions. Am. J. Cardiol. 101(10A) 20D-29D. [Pg.280]

In summary, Caco-2 cells studies strongly suggest that carotenoids interact with each other at the level of cellular uptake by the enterocyte. This phenomenon has been explained by the fact that the uptake of several carotenoids involves, at least in part, the same intestinal membrane transporter the scavenger receptor class B type ISR-BI (Reboul et al. 2005, van Bennekum et al. 2005, Moussa et al. 2008). [Pg.383]

Structural information about the oxygenases provided limited insight into the mechanism (Schmidt et al. 2006). The crystallized enzyme from Synechocystis sp. PCC6803 is membrane associated and the interaction with the membrane is believed to be mediated by a nonpolar patch on the surface of the enzyme. This hydrophobic patch is thought to provide the necessary access of the protein to the membrane-bound carotenoids. Following withdrawal from the membrane, the substrate moves through the hydrophobic tunnel toward the metal center. The substrate orients the... [Pg.403]


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Interaction membranes

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