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Membranes Osborne

Botulism neurotoxins bind with synaptic vesicular proteins and block the release of acetylcholine from the presynaptic membrane (Osborne et al, 2007). Clinical signs of botulism are weakness, tremors, recumbency, laryngeal paresis, and other signs of nervous system dysfunction (Braun et al, 2005). Botulism toxins do not appear to be excreted in milk (Galey et al, 2000). [Pg.741]

Nunnari J, Fox TD, Walter P (1993) A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 262 1997-2004 Osborne AR, Rapoport , van den Berg (2005) Protein translocation by the Sec61/SecY channel. Annu Rev Cell Dev Biol 21 529-550 Paschen SA, Neupert W, Rapaport D (2005) Biogenesis of beta-barrel membrane proteins of mitochondria. Trends Biochem Sci 30 575-582 Paschen SA et al. (2003) Evolutionary conservation of biogenesis of beta-barrel membrane proteins. Nature 426 862-866... [Pg.70]

Heath, D. D. Osborn, P. J. (1976). Formation of Echinococcus granulosus laminated membrane in a defined medium. International Journal for Parasitology, 6 467-71. [Pg.325]

In addition to the traditional dermal delivery formulations discussed above, several other pharmaceutical semi-solid and liquid formulation types have been the subject of a considerable amount of R D. These include sprays, foams, multiple emulsions, microemulsions, liposomal formulations, niosomes, cyclodextrins, glycospheres, dermal membrane structures and microsponges. Although some of these formulations form part of the pharmaceutical armamentarium, they are yet to achieve widespread application and are not within the scope of this chapter. The interested reader is referred to the excellent coverage by Osborne and Amann (1990), Kreuter (1994) and Liu and Wisniewski (1997). [Pg.556]

Osborne, H.B., Nabedryk-Viala, E. (1978) The conformation of membrane-bound rmd detergent-solubiUsed bovine rhodopsin. A comparative hydrogen-isotope exchange study. European Journal of Biochemistry, 89 (1), 81—88. [Pg.15]

Tagawa ST, Beltran H, VaUabhajosula S, Goldsmith SJ, Osborne J, Matulich D, et al. Anti-prostate-Specific membrane antigen-based radioimmnnotherapy for prostate cancer. Cancer. 2010 116(S4) 1075-83. [Pg.38]

Several firms participated in the development of the membrane cell. Conceptual studies of permselective membranes began in the mid-1940s. W. Juda et al. of Ionics Corporation, and S.G. Osborne of Hooker Chemical hold early patents (1950s) on the membrane-cell process [35]. [Pg.32]

Like Diamond, Hooker Chemicals demonstrated an interest in ion-exchange membranes since the mid-1940s. S.G. Osborne etal. of Hooker Chemical Corporation hold the original patent for the first membrane cell [36]. This patent was filed on January 23,1952. With this patent. Hooker embarked upon a major development program until 1957. Following a period of relative inactivity, the Nafion membrane rekindled interest in membrane-cell technology. [Pg.33]

Osborne D.J., Boubriak L, Leprince O. (2002). Rehydration of Dried Systems Membranes and the Nuclear genome. In Desiccation and Survival in Plants Drying Without Dying, Black M. Pritchard H. W. (Ed.), pp. 343-366, CABl Publishing, New York, USA, ISBN 0 85199 534 9... [Pg.18]

Intermediate filaments of 7-11 run diameter (Weber and Osborn 1982) of the vimentin type (Franks et al. 1979) are arranged immediately around the cell nucleus, while the remaining cytoplasm reveals only small amounts of 10 mn filaments, which usually do not extend up to the outer membrane of the mononuclear phagocyte (Cain et al. 1982, 1983). With increasing differentiation of monocytes into mature macrophages and epithelioid cell equivalents, a loosening up of the perinuclear vimentin filament network was observed. This development was associated with a straightening of the filaments, which could now be followed into the ectoplasm and into the cytoplasmic processes. [Pg.250]

Lee HJ, Beattie PD, Seddon BJ, Osborne MD, Girault HH (1997) Amperometric ion sensors based on laser-patterned composite polymer membranes. J Electroanal Chem 440 73... [Pg.632]

Schindler, M., Osborn, M.J., Koppel, D.E. Lateral diffusion of lipopolysaccharide in the outer membrane of Salmonella typhimurium. Nature 285, 261-263 (1980)... [Pg.290]

Mulford, C. A., and Osborn, M. J. (1983). An intermediate step in translocation of lipo-polysaccharide to the outer membrane of Salmonella typhimurium. Proc. Natl Acad. Sci. USA 80, 1159-1163. [Pg.1563]

Osborn, M. J. (1979). Biosynthesis and assembly of the lipopolysaccharide of the outer membrane. In Bacterial Outer Membranes, M. Inouye, ed. (New York Wiley), pp. 15-34. [Pg.1564]

Edelhoch, H., and Osborne, J. C., 1976, The thermodynamic basis of the stability of proteins, nucleic acids, and membranes, Adv. Protein Chem. 30 183. [Pg.91]

Osborn et al have shown that synthesis of lipopolysaccharide in S. typhimurium takes place exclusively in the cytoplasmic membrane. The specific pulse label (1 min at 25 C) of the polysaccharide chain (O-antigen) of the lipopolysaccharide initially appeared in the cytoplasmic membrane and was then rapidly transferred to the outer membrane during a subsequent chase. The mechanism of translocation of the completed lipopolysaccharide from the cytoplasmic membrane to the outer membrane is not yet clear. However, it has been shown by MUhlradt et al. that newly synthesized lipopolysaccharide is translocated at a few, localized sites on the S. typhimurium cell surface. These authors found that after a 30-sec pulse label with [ C]galactose, new lipopolysaccharide appeared at about 220 sites on the cell surface, and within 2-3 min, it was evenly distributed over the entire cell surface. When ultrathin sections of plasmolyzed cells were examined under the electron microscope after pulse labeling, newly synthesized lipopolysaccharide was found to be located above sites where the cytoplasmic and outer membranes were attached to each other. Such bridges between the two membranes may provide for the translocation of the newly synthesized lipopolysaccharide (see also Chapter 11). [Pg.367]

The chemical mediator at insect ganglia is acetylcholine which is abundantly present in the brain. The mediator at the neuromuscular junction is not acetylcholine, as in mammals, but L-glutamic acid (7.57) (Clements and May, 1974 Irving, Osborne, and Wilson, 1976), and for this neurotransmitter, no selective antagonist has yet been found. The receptors for both neurotransmitters are well protected by selectively permeable membranes. [Pg.270]


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