145 research outputs found
Interpretation of the Multiplicity of Kinetics in Heterogeneous Catalysis*
application/pdfThe multiplicity of reaction kinetics in heterogeneous catalysis has been studied by using the oxidation of propene over Pt/SiO_2 of widely varying dispersion, relating to the adsorption behavior of reaction components at temperature a range of 290?350℃. The reaction consists of a partial oxidation to propanal and complete oxidation to CO_2 and H_20, each of which progresses independently in parallel on own active sites. The rate of propanal formation indicates a characteristic oscillation. The oscillation seems to be a multiplicity caused by the switching between two different surface structures on each of which the partial oxidation progresses at different rate, high rate (γCHO^H) and low rate (γCHO^L). For γCHO^H andγCHO^L, the L-H and E-R models consistently explained all experimental data. Three rate equations for the two rates to form propanal and the complete oxidation are expressed γCHO^H =κCHO^HPc_3H_6^Pn_2O^ γ^=κCHO^LPc_3H_6^Pn_2O^ γCO_2=κCO_2Pc_3H_6^Pn_2O^ The activation energies for propanal formation at high and low rates and for CO_2 formation were evaluated to be 9(±4)kJ/mol 92?218kJ/mol and 85(±5)kJ/mol, respectively. All the surface coverages of N_20, C_3H_6 and propanal during the reaction were evaluated to be θN_2O=0.13, θC_3H_6=0.69?1.17 and θCHO=0.15, respectively. θC_3H_6 is presumed to be a sort of trigger for the oscillating rate.departmental bulletin pape
Antimicrobial Activity and Protease Stability of Peptides Containing Fluorinated Amino Acids
Selective fluorination of peptides results in increased chemical and thermal stability with
simultaneously enhanced hydrophobicity. We demonstrate here that fluorinated derivatives of two host
defense antimicrobial peptides, buforin and magainin, display moderately better protease stability while
retaining, or exhibiting significantly increased bacteriostatic activity. Four fluorinated analogues in the buforin
and two in the magainin series were prepared and analyzed for (1) their ability to resist hydrolytic cleavage
by trypsin; (2) their antimicrobial activity against both Gram-positive and Gram-negative bacterial strains;
and (3) their hemolytic activity. All but one fluorinated peptide (M2F5) showed retention, or significant
enhancement, of antimicrobial activity. The peptides also showed modest increases in protease resistance,
relative to the parent peptides. Only one of the six fluorinated peptides (BII1F2) was degraded by trypsin
at a slightly faster rate than the parent peptide. Hemolytic activity of peptides in the buforin series was
essentially null, while fluorinated magainin analogues displayed an increase in hemolysis compared to the
parent peptides. These results suggest that fluorination may be an effective strategy to increase the stability
of biologically active peptides where proteolytic degradation limits therapeutic value
Correlations of R<sub>10</sub> with the variations of SOC, soil TN, and soil P in broadleaved and mixed forests.
<p>Correlations of R<sub>10</sub> with the variations of SOC, soil TN, and soil P in broadleaved and mixed forests.</p
Relationships of Q<sub>10</sub> with variation of herbaceous carbon stock in both forest types.
<p>Relationships of Q<sub>10</sub> with variation of herbaceous carbon stock in both forest types.</p
Variation in basal parameters of soil respiration within or between forest types.
<p>The significance of differences of basal parameters between forest types were separately tested by independent t - test (two - tailed) at α = 0.05 (n = 9 in the broadleaved forest, and 11 in the mixed forest). Same lowercase letter means no significant difference is detected at α = 0.05 within 95% confidence interval between the two forest types.</p
Relationships between soil chemical properties and Q<sub>10</sub> respectively in broadleaved and mixed forest types.
<p>Relationships between soil chemical properties and Q<sub>10</sub> respectively in broadleaved and mixed forest types.</p
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