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Escherichia coli stability

Sandhu, P., Guo, Z., Baba, T., Martin, M. V., Tukey, R. H., and Guengerich, F. P., 1994, Expression of modified human cytochrome P450 1A2 in Escherichia coli stabilization, purification. [Pg.314]

R.H. Tukey, and F.P. Guengerich (1994). Expression of modified human cytochrome P450 1A2 in Escherichia coli Stabilization, purification, spectral characterization, and catalytic activities of the enzyme. Biochem. Biophys. 309, 168-177. [Pg.472]

Parasitism can serve to regulate competition between different host populations. An example is provided by the work of Levin et al. (76). They found that parasitism by the virulent bacteriophage T2 on two strains of Escherichia coli stabilized the competition of the strains for sugar, and allowed the competitors to coexist in a chemostat. One of the strains was susceptible to infection by T2 but the other was not. [Pg.221]

Taylor FR, Cronan JE Jr. Cyclopropane fatty acid synthase of Escherichia coli. Stabilization, purification, and interaction with phospholipid vesicles. Biochemistry 1979 18 3292-3300... [Pg.110]

An examination of mutant PKA proteins was undertaken. Phosphorylation of Thr-197 is required to activate PKA and phosphorylation of Ser-338 enhances stability of the protein. Replacement of Thr-197 and/or Ser-338 by Ala was examined to determine any conformational changes in the protein. Both single substitution mutants were expressed in Escherichia coli in similar levels to wild-type protein. However, both mutants were found to be less stable, as had been previously described. The double mutant... [Pg.26]

Langsetmo K, Fuchs JA, Woodward C (1991) The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. its titration produces a related shift in global stability Biochemistry 30 7603-7609. [Pg.281]

Table 8.1 Temperature stability of Rhodococcus rhodochrous J1E/393G mutant NHase compared with J1 NHase, each expressed in Escherichia coli JM109... Table 8.1 Temperature stability of Rhodococcus rhodochrous J1E/393G mutant NHase compared with J1 NHase, each expressed in Escherichia coli JM109...
Yazdani, S. and Mukherjee, K. (2004) Continuous-culture studies on the stability and expression of recombinant streptokinase in Escherichia coli. Bioprocess and Biosystems Engineering, 24, 341-346. [Pg.282]

Stabilizer of iron Escherichia coli 1VH4 1.5 Badger... [Pg.63]

Immobilization—stabilization of penicilhn G acylase from Escherichia coli. Appl. Biochem. Biotechnol., 26, 181-196. [Pg.335]

Ginsburg, A. Szczepanowski, R.H. Ruvinov, S.B. Nosworthy, N.J. Sondej, M. Umland, T.C. Peterkofsky, A. Conformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate sugar phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189 implications for phosphorylation effects. Protein Sci., 9, 1085-1094 (2000)... [Pg.422]

Fig. 8. Stability of the rhamnulose 1-phosphate aldolase from Escherichia coli (RhuA) vs. that of the fructose 1,6-bisphosphate aldolase from rabbit muscle (FruA) in phosphate buffer (pH 7.2 25°C ca. 1 Uml ) a) RhuA b) O RhuA, 30% EtOH c) RhuA, 50% DMSO d) FruA... Fig. 8. Stability of the rhamnulose 1-phosphate aldolase from Escherichia coli (RhuA) vs. that of the fructose 1,6-bisphosphate aldolase from rabbit muscle (FruA) in phosphate buffer (pH 7.2 25°C ca. 1 Uml ) a) RhuA b) O RhuA, 30% EtOH c) RhuA, 50% DMSO d) FruA...
Figure 4. The technique of serial transfer. An RNA sample which is capable of replication in the assay is transferred into a test-tube containing stock solution. This medium contains the four nucleoside triphosphates (ATP, UTP, GTP and CTPJand a virus specific RNA polymerase, commonly QP-replicase because of the stability of this protein, in a suitable buffer solution. RNA replication starts instantaneously. After a given period of time a small sample is transferred to the next test-tube and this procedure is repeated about one hundred times. The transfer has two consequences (i) the material consumed in the replication is replaced, and (ii) the distribution of RNA variants is subjected to a constraint selecting for the fastest replicating species. Indeed, the rate of replication is increased by several orders of magnitude in serial transfer experiments starting out from natural QB RNA and leading to variants that are exclusively suited for fast replication and hence are unable to infect their natural hosts, Escherichia coli. Figure 4. The technique of serial transfer. An RNA sample which is capable of replication in the assay is transferred into a test-tube containing stock solution. This medium contains the four nucleoside triphosphates (ATP, UTP, GTP and CTPJand a virus specific RNA polymerase, commonly QP-replicase because of the stability of this protein, in a suitable buffer solution. RNA replication starts instantaneously. After a given period of time a small sample is transferred to the next test-tube and this procedure is repeated about one hundred times. The transfer has two consequences (i) the material consumed in the replication is replaced, and (ii) the distribution of RNA variants is subjected to a constraint selecting for the fastest replicating species. Indeed, the rate of replication is increased by several orders of magnitude in serial transfer experiments starting out from natural QB RNA and leading to variants that are exclusively suited for fast replication and hence are unable to infect their natural hosts, Escherichia coli.
Escherichia coli (Niehaus, 1999). Whereas halophiles (Margesin, 2001) and piezo-philes (Abe, 2001) have attracted attention, the main aspect of interest for biotechnological application remains thermal stability, focusing interest on thermophiles or even hyperthermophiles. Increase in temperature has a significant influence on the bioavailability and solubility of organic compounds (not on the solubility of Oz, however, which is nearly zero at extremophilic temperatures ). Current applications of extremozymes include ... [Pg.55]

Protein expression and purification have traditionally been time-consuming, case-specific endeavors, and are considered to be the greatest bottlenecks in most proteomics pipelines (1) Escherichia coli (E. coli) is the most convenient and cost-effective host, although optimal conditions for the expression of different proteins vary widely. Proteins vary in their structural stability, solubility, and toxicity in this environment, resulting in differing rates of protein degradation,... [Pg.115]

Henner.W.D., I. Kleber, and R. Benzinger. 1973. Transfection of Escherichia coli spheroplasts. 3. Facilitation of transfection and stabilization of spheroplasts by different basic polymers./. Virol. 12 741—747. [Pg.140]


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See also in sourсe #XX -- [ Pg.319 , Pg.320 ]




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