Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Cold adaptation

Live attenuated vaccines for RSV are also being developed. Most of these vaccine candidates are derived from cold adaptation, by passing the vims at progressingly lower temperatures than human body temperatures. However, other means of mutagenesis have been used to generate vaccine candidates (72). Several clinical trials of these vaccines are also in progress (73,74). [Pg.359]

Influenza. Although current influenza vaccine (subunit spHt vaccine) has been in use yearly for the elderly, it is not recommended for the general population or infants. Improvements to increase or prolong the immunogenicity, reduce the side-effects (due to egg production procedure), and provide mass protection are stiU being pursued. One approach is to use a five, attenuated vims though cold adaptation. A vaccine has been used in Russia and demonstrated to be safe and efficacious for infants (82). Clinical trials for a similar vaccine are being carried out in the United States (83). [Pg.359]

Nichols DS, MR Miller, NW Davies, A Goodchild, M Raferty, R Caviccholi (2004) Cold adaptation in the Antarctic arch eon Methanococcoides burtonii involves membrane lipid unsaturation. J Bacterial 186 8508-8515. [Pg.179]

Margesin R, F Schinner (1997) Efficiency of indigenous and inoculated cold-adapted soil microorganisms for biodegradation of diesel oil in alpine oils. Appl Environ Microbiol 63 2660-2664. [Pg.643]

Several studies gave rise to a general view of seasonality in aquatic insect emergence. Cold-adapted insect taxa such as Diamesinae tend to dominate emergence in... [Pg.207]

Measles/mumps/rnbella Varicella zoster Influenza (cold-adapted) Influenza ... [Pg.319]

Additional information <1, 2, 58> (<58> high specific activity at low temperature, cold-adapted organism [68]) [1, 2, 68]... [Pg.294]

Additional information <1, 7, 9, 13, 25, 26, 50, 58> (<58> decreased thermostability, cold-adapted organism [68] <58> the recombinant His-tagged wild-type enzyme shows reduced thermostability compared to the native and recombinant wild-type without tag [62] <25> thermal denaturation at pH 5.5 and pH 7.5 of the isoenzymes [33] <1> PGKl is more heat-stable than PGK2... [Pg.307]

Laurberg P, Andersen S, Karmisholt J. Cold adaptation and thyroid hormone metabolism. Horrn Metab Res. 2005 37 545-549. [Pg.412]

The results of studies using a wide range of oxidizable substrates showed that, in fact, there was a modicum of temperature compensation, but that it was nothing like the metabolic cold adaptation originally envisaged. Some thermal compensation was also achieved by increasing the density of cristae within the mitochondria, but this was of less importance than actual mitochondrial density. [Pg.10]

Studies by Johnston and Roots (1964), Roots (1968) and Kreps (1981) have revealed an increased ratio between the plasmalogenic and diacyl forms of phosphatidyl ethanolamine in oceanic fish from low-temperature waters. During cold adaptation, the ratios between the main phospholipid fractions alter the relative proportion of phosphatidyl choline decrease and phosphatidyl ethanolamine, phosphatidyl serine and sphingomyelin, all of which contain large amounts of polyenoic acids, increase (Caldwell and Vemberg, 1970 Miller etal, 1976 Wodke, 1978 Hazel, 1979 Brichon et al., 1980 van den Thillart and de Bruin, 1981 Zabelinsky and Shukolyukova, 1989). [Pg.18]

Haschemeyer, A.E.V. (1980). Temperature effects on protein metabolism in cold-adapted fishes. Antarctic Journal of the United States 15,147-149. [Pg.275]

Holeton, G.F. (1974), Metabolic cold adaptation of polar fish fact or artefact Physiological Zoology 47,137-152. [Pg.277]

Somero, G.N., Giese, A.C. and Wohlschlag, D.E. (1968). Cold adaptation of the Antarctic fish Trematomus bemacchii. Comparative Biochemistry and Physiology 26,223-233. [Pg.314]

Wohlschlag, D.E. (1960). Metabolism of an Antarctic fish and the phenomenon of cold adaptation. Ecology 41,287-292. [Pg.322]

Rozman K, Greim H. 1986. Toxicity of 2,3,7,8-tetrachlorodibenzo-p-dioxin in cold-adapted rats. Arch Toxicol 59 211-215. [Pg.680]

Further pharmacological effects of deltorphins have been demonstrated under various experimental conditions. D-Ala-deltorphin improves memory consolidation in a passive avoidance apparatus in mice this effect is abolished by naltrindole [75]. D-Ala-deltorphin-II caused hypothermia in cold-adapted animals [76]. In contrast to mu opiate agonists, D-Ala-deltorphin-I, at low doses, stimulates respiratory activity in fetal lambs, and this effect is blocked by simultaneous administration of naltrindole [77], The peptide D-Ala-deltorphin-II inhibits diarrhea induced by castor oil and colonic bead expulsion, but it leaves the rate of transit through the small intestine unchanged [78,79]. By the SC route D-Ala-deltorphin-I inhibits acidified alcohol-induced gastric mucosal lesions [80], but by the ICV route, it fails to affect gastric secretion [81], The peptide is involved also in the control of ingestive behavior. It stimulates the intake of food [82] and of sucrose [83],... [Pg.184]

Three mutants with improved activity at 10°C were identified in the first generation library. Recombination of these resulted in variant (P3C9) whose k,M at 10°C is 6.6 times that of wild-type SSII and 4.5 times that of the naturally cold-adapted S41 (Fig. 17). The mutant SSII Km is 9.6 times that of wild type and 6.6 times S41 s (Table II). The activities of naturally psychrophilic enzymes are generally less temperature dependent than those of their mesophilic counterparts. The temperature dependence of enzyme activity is often expressed in terms of the increase in kcM brought about by raising the reaction temperature by 10°C ( (Tjo ) The (Tjo of P3C9 is —1.2, more than two times lower than wild-type SSII and comparable to the value of—1.3 determined for S41. [Pg.199]

Kano, H., Taguchi, S., and Momose, H. (1997). Cold adaptation of a mesophilic serine protease, subtilisin, by in vitro random mutagenesis. Appl. Microbiol. Biotechnol, 47, 46-51. [Pg.289]

Taguchi, S., Ozaki, A., and Momose, H. (1998). Engineering of a cold-adapted protease by sequential random mutagenesis and a screening system. Appl. Environmental Microbiol., 64(2), 492-495. [Pg.291]

Corsaro, M.M., Pieretti, G., Lindner, B., Lanzetta, R., ParriUi, E., Tutino, M.L., Parrilli, M. Highly phosphorylated core oligosaccharide structures from cold-adapted Psychromonas arctica, Chem Eur J 14 (2008) 9368-937. [Pg.94]


See other pages where Cold adaptation is mentioned: [Pg.700]    [Pg.387]    [Pg.296]    [Pg.157]    [Pg.157]    [Pg.68]    [Pg.69]    [Pg.222]    [Pg.1660]    [Pg.88]    [Pg.199]    [Pg.168]    [Pg.199]    [Pg.206]    [Pg.207]    [Pg.301]    [Pg.303]    [Pg.303]    [Pg.304]    [Pg.304]    [Pg.307]    [Pg.307]    [Pg.307]    [Pg.310]    [Pg.311]    [Pg.312]    [Pg.313]    [Pg.313]    [Pg.314]    [Pg.314]   


SEARCH



© 2024 chempedia.info