The chemistry and catalysis of the water/toluene reaction 1. The specific activities and selectivities of the Group VIII metals supported on Al2O3

1978 ◽  
Vol 51 (2) ◽  
pp. 203-211 ◽  
Author(s):  
D GRENOBLE
1973 ◽  
Vol 51 (24) ◽  
pp. 4031-4037 ◽  
Author(s):  
Norman Henry Sagert ◽  
Rita Mary Louise Pouteau

Specific activities of Group VIII noble metals supported on Graphon have been determined for hydrogen–water deuterium exchange. Metal surface areas, which are required to calculate specific activities, were measured by hydrogen chemisorption, and by reaction of hydrogen with chemisorbed oxygen. For the second triad metals, ruthenium, rhodium, and palladium, and in the temperature range 140 to 225 °C, the variation of activity was Ru < Rh > Pd. For the third triad metals, osmium, iridium, and platinum, the variation of activities was Os < Ir < Pt in the same range of temperature. Apparent activation energies were measured over this temperature range, and orders of reaction with respect to hydrogen and water were measured at 160 °C (200 °C for Pt). From these data, activation energies for the surface exchange reaction were calculated. In the second triad the activation energies decrease slightly with increasing atomic number, but in the third triad they decrease quite markedly with increasing atomic number. A good correlation was obtained between the activation energy for surface exchange and the thermionic work function of the metal. This supports our earlier suggestion that Graphon is able to donate electrons to the metal and thus lower the activation energy for the surface exchange.


1974 ◽  
Vol 52 (16) ◽  
pp. 2960-2967 ◽  
Author(s):  
Norman H. Sagert ◽  
Rita M. L. Pouteau

Specific activities of unsupported powders of all six Group VIII noble metals have been determined for hydrogen – water deuterium isotope exchange. The metal surface areas, which are required to calculate the specific activities were measured by hydrogen chemisorption and were checked by electron microscopy. Specific activities were measured as a function of temperature in the range 353 to 573 K and also as a function of the partial pressure of hydrogen and water at suitable temperatures and over a tenfold range of partial pressures.The variation in the specific activities was Pd < Ir ≤ Ru < Rh < Os < Pt, and these specific activities varied over a range of about 1000. The observed orders with respect to hydrogen and water are shown to be consistent with a mechanism in which chemisorbed hydrogen atoms exchange with physically adsorbed water.From the orders and the apparent activation energies, the chemical activation energies (E0) were calculated. These varied randomly within the range 61 ± 6 kJ mol−1 for all the metals studied. Previously we showed that there was a correlation of E0 with the work function of the metal when metals were supported on a highly graphitized carbon black, and suggested that electron donation from the carbon to the metal was responsible for the correlation. This suggestion is supported by the present results which show that E0 is relatively constant for all six metals in the absence of a support.


1993 ◽  
Vol 69 (05) ◽  
pp. 430-435 ◽  
Author(s):  
Colin Longstaff ◽  
Man-Yu Wong ◽  
Patrick J Gaffney

SummaryAn international collaborative study has been carried out to investigate the reproducibility of hirudin assays in 13 laboratories using four recombinant hirudins and one natural, sulphated product. A simple assay procedure was proposed involving the titration of α-thrombin with inhibitor and measurement of residual activity using a chromogenic substrate. A standard α-thrombin preparation was supplied to ensure that this reagent was of uniform quality throughout the study. The method appeared to present no difficulties and laboratories reported similar potencies for the 5 hirudin samples, in line with expected values. This gave 200–222 Thrombin Inhibitory Units/ampoule (TIU/ampoule) of lyophilised hirudin, with geometric coefficient of variation (gcv) values ranging from 10.15–15.97%. This corresponds to specific activities of approximately 14,300–15,900 TIU/mg protein. This is close to the upper limit of previously reported values of specific activity. We conclude that the precision of this determination compared with the wider range of values in the literature (8,000–16,000 thrombin inhibitory units [TIU]/mg) results from the use of good quality standard α-thrombin by all laboratories. This study has important implications for hirudin standardisation.


1996 ◽  
Vol 76 (03) ◽  
pp. 361-368 ◽  
Author(s):  
Carrie H Fang ◽  
T-C Lin ◽  
Arabinda Guha ◽  
Yale Nemerson ◽  
William H Konigsberg

SummaryIn an attempt to define sequence elements in human and mouse tissue factor (TF) that are responsible for the species specificity observed in their interaction with human factor VIIa (HVIIa), we constructed human-mouse chimeric TF cDNAs, inserted them into plasmid vectors, and induced their expression in E.coli. Assays for procoagulant activity were carried out with the resulting E. coli lysates using (HVIIa) human and mouse (MVIIa). The ratio of the procoagulant activities, HVIIa/MVIIa, revealed that human TF exon 3 was essential for activity when the TF:VIIa complex was formed with HVIIa. By ligating the maltose binding protein (MBP) gene to TF cDNAs it was possible to construct, express and purify MBP-TF chimeras as well as to estimate their specific activities. With selected MBP-TF chimeras and HVIIa we determined kinetic parameters for the activation of human factor X. Replacement of exon 3 in human TF cDNA with the corresponding exon from mouse TF cDNA resulted in both lower affinity for HVIIa and failure to convert bound HVIIa into a potent protease


1972 ◽  
Vol 71 (1) ◽  
pp. 24-36 ◽  
Author(s):  
Ariel Gordin ◽  
Pirkko Saarinen

ABSTRACT An account is given of a methodological study of the double-antibody radioimmunoassay of human TSH, using highly purified labelled human TSH as tracer. It was shown that conventional paper electrophoresis was not adequate for studying the purity of labelled human TSH. When polyvinylchloride (Pevikon®) electrophoresis was used, four subfractions could still be separated, even though, on paper electrophoresis, the material seemed to be homogeneous. Only two of the four Pevikon fractions were immunoreactive. Purification of labelled human TSH by Pevikon electrophoresis also improved the sensitivity of the assay. Specific activities of about 100 mCi/mg gave the highest initial binding capacity, produced least damage to the labelled hormone and showed the best stability of the tracer without influencing the sensitivity of the method. In different storage conditions, labelled human TSH was found to be most stable at −20°C and diluted 1/100. Only in pregnancy did the addition of HCG seem necessary. The mean TSH value in healthy subjects was 3.6 ± 1.4 μU/ml (mean±sd) with a range from 1.6 μU/ml to 8.8 μU/ml.


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