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Gel profile

Fig. 13. The nuclear magnetic spin-lattice relaxation rate for water protons as a function of magnetic field strength reported as the proton Larmor frequency at 298 K for 5% suspensions of the particulate stabilized in a 0.5% agar gel presented as the difference plot (A) Zeolite 3A (B) Zeolite 13X (C) Zeolite NaY (D) kaolin with 7 s added to each point to offset the data presentation (E) Cancrinite with 9 s added to each point to offset the data presentation and (F) 0.5% agar gel profile with 10 s added to each point. The solid lines are fits to a power law (68). Fig. 13. The nuclear magnetic spin-lattice relaxation rate for water protons as a function of magnetic field strength reported as the proton Larmor frequency at 298 K for 5% suspensions of the particulate stabilized in a 0.5% agar gel presented as the difference plot (A) Zeolite 3A (B) Zeolite 13X (C) Zeolite NaY (D) kaolin with 7 s added to each point to offset the data presentation (E) Cancrinite with 9 s added to each point to offset the data presentation and (F) 0.5% agar gel profile with 10 s added to each point. The solid lines are fits to a power law (68).
Figure 4. Rise and gel profiles, Formulation A. Key -----------, rise rate ----,... Figure 4. Rise and gel profiles, Formulation A. Key -----------, rise rate ----,...
In Figure 9, the rate of evolution of carbon dioxide from formulation "A" is compared with the rise and "gel profiles" for this formulation. A maximum in cell-opening is measured before full rise height is achieved and at the time of an inflexion in the rise-rate curve. This maximum in the rate of cell-opening happens while the processes measured by "gel profile" are occurring. [Pg.139]

Figure 9. Comparison of the rise profile and gel" profile of Formulation A with the evolution of carbon dioxide measured by infrared absorbance at 2320 cm 1. Figure 9. Comparison of the rise profile and gel" profile of Formulation A with the evolution of carbon dioxide measured by infrared absorbance at 2320 cm 1.
In Figure 17, the absorbance due to substituted ureas at 1645 cm" for the three formulation at early times of reaction are given as functions of time. These data are compared with the rise profile, gel profile and cell-opening times previously discussed, Figures 4-10. Concentrations of ureas are measurable from about the time of the peak rate of foam rise and achieve an apparently limiting value after about four minutes, about the time foam rise is complete. "Gel profile" appears to monitor structural developments in the foams which are occurring at the same time as the increase in urea concentration. In the "HR" formulation, onset of "gel" is delayed. This delay in onset of "gel" in high resiliency foams has often been observed (X, ]). [Pg.142]

No such delay, however, is observed in formation of diarylurea. While no direct measurement is yet available, it is taken that "gel profile" measures association of the polyureas into domains. In "HR" foams this domain formation is delayed, permitting larger, more completely aligned polyurea domains and accounting for the principal property characteristics which distinguish high resiliency foam 3). [Pg.142]

The objective of these studies has been to develop a reaction sequence model for flexible urethane foam which would account for the physical stages in the foaming process evident from foam rise measurements. In Figure 18, a generalized rise profile and gel profile" is used to summarize the reaction sequence model. [Pg.146]

Figure 18. General summary of rise and gel profiles indicating the stages evident in the physical formation of foam and the sequence of chemical reactions occurring. Figure 18. General summary of rise and gel profiles indicating the stages evident in the physical formation of foam and the sequence of chemical reactions occurring.
Marvaldi, J., and Lucas-Lenard, J., 1977, Differences in the ribosomal protein gel profile after infection of L cells with wild-type or temperature-sensitive mutants of vesicular stomatitis virus. Biochemistry 16 4320. [Pg.289]

Fig. 4. Double-label gel profiles of isolated mitochondria obtained during petite induction. Log-phase cultures of 55-R5-3C and 1121 were grown on 2% galactose for 5-6 doublings at 18°C (A), or at 28°C in the presence of 3 mg per ml of chloramphenicol (B), and were labeled with [ H]leucine or [ C]leucine in the presence of 200 Mg per ml cycloheximide. After labeling, mitochondria were isolated and the protein was separated on 10% SDS polyacrylamide gels. After electrophoresis, the gels were sliced and counted. The data are normalized to the total radioactivity recovered from the gels after correction for spillover of the two isotopes. (From Weislogel and Butow. )... Fig. 4. Double-label gel profiles of isolated mitochondria obtained during petite induction. Log-phase cultures of 55-R5-3C and 1121 were grown on 2% galactose for 5-6 doublings at 18°C (A), or at 28°C in the presence of 3 mg per ml of chloramphenicol (B), and were labeled with [ H]leucine or [ C]leucine in the presence of 200 Mg per ml cycloheximide. After labeling, mitochondria were isolated and the protein was separated on 10% SDS polyacrylamide gels. After electrophoresis, the gels were sliced and counted. The data are normalized to the total radioactivity recovered from the gels after correction for spillover of the two isotopes. (From Weislogel and Butow. )...
Fig. 8. Double-label gel profile of mitochondria from 650-2C and 24. Cells were grown at 28° C or 18°C on 2% galactose, harvested at early stationary phase, and labeled for 1 h (28°C) or 2 h (18°C) in the presence of 600 Mg/ml of cycloheximide with [ C]leucine (650-2C) or [ H]leucine (24). Proteins were separated on 10% SDS polyacrylamide gels, sliced, and counted for radioactivity. (From Butow et al. )... Fig. 8. Double-label gel profile of mitochondria from 650-2C and 24. Cells were grown at 28° C or 18°C on 2% galactose, harvested at early stationary phase, and labeled for 1 h (28°C) or 2 h (18°C) in the presence of 600 Mg/ml of cycloheximide with [ C]leucine (650-2C) or [ H]leucine (24). Proteins were separated on 10% SDS polyacrylamide gels, sliced, and counted for radioactivity. (From Butow et al. )...
Fig. 9. Double-label gel profile of mitochondria isolated from 650-2C and 49. Cells were grown and labeled as in Fig. 8 650-2C, [ CJleucine 49, PHJleucine. (From Butow et... Fig. 9. Double-label gel profile of mitochondria isolated from 650-2C and 49. Cells were grown and labeled as in Fig. 8 650-2C, [ CJleucine 49, PHJleucine. (From Butow et...
Fig. 4. Electrophoretic (acrylamide gel) profiles of radioactivity of proteins extracted from Strongyhcentrotus purpuratus embryos after incorporation of l-valine- C at (I) 3-4 hours and at (II) 23-24 hours after fertilization, cultured with (lA and IIA) and without (IC and IIC) actinomycin D (20 /ig/ml) protein content per 0.25 ml sample for lA, IC, IIA, and IIC = 0.40, 0.35, 0.26, and 0.46 mg, respectively total radioactivity in protein per applied sample for lA, IC, IIA, and IIC = 39,800, 38,200, 22,275, and 15,900 cpm, respectively. Numbers (1-7) indicate repeatedly identifiable peaks. From Spiegel et al. (1965). Fig. 4. Electrophoretic (acrylamide gel) profiles of radioactivity of proteins extracted from Strongyhcentrotus purpuratus embryos after incorporation of l-valine- C at (I) 3-4 hours and at (II) 23-24 hours after fertilization, cultured with (lA and IIA) and without (IC and IIC) actinomycin D (20 /ig/ml) protein content per 0.25 ml sample for lA, IC, IIA, and IIC = 0.40, 0.35, 0.26, and 0.46 mg, respectively total radioactivity in protein per applied sample for lA, IC, IIA, and IIC = 39,800, 38,200, 22,275, and 15,900 cpm, respectively. Numbers (1-7) indicate repeatedly identifiable peaks. From Spiegel et al. (1965).

See other pages where Gel profile is mentioned: [Pg.625]    [Pg.35]    [Pg.80]    [Pg.41]    [Pg.450]    [Pg.18]    [Pg.299]    [Pg.195]    [Pg.460]    [Pg.133]    [Pg.136]    [Pg.137]    [Pg.137]    [Pg.137]    [Pg.140]    [Pg.112]    [Pg.136]    [Pg.22]    [Pg.23]    [Pg.672]    [Pg.161]   
See also in sourсe #XX -- [ Pg.133 ]




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