Kinetic studies on a Ziegler catalyst system

1959 ◽  
Vol 34 (127) ◽  
pp. 49-63 ◽  
Author(s):  
A. Gilchrist

The kinetics of the Ziegler-catalyzed polymerization of ethylene have been studied in a static system in the complete absence of any hydrocarbon vehicle. The apparatus which was developed consisted essentially of two mixing vessels, each of which was connected to the reaction vessel and to various manometric devices. Two mixtures were prepared: one of ethylene and aluminium trimethyl vapour and one of ethylene and titanium tetrachloride vapour. The fall in pressure due to the polymerization reaction was recorded. The dependence of the rate of polymerization on catalyst concentration and composition has been established. An optimum catalyst ratio was found at an Al/Ti mole ratio of 2:1. The rate of polymerization was concluded to be independent of the amount of aluminium trimethyl present over a large range of alkyl concentration. The kinetic order with respect to total pressure was found to be non-integral. It has been shown, moreover, that the effective catalyst concentration decreases during any given run. By employing a kinetic technique the effect of changing catalyst concentration has been removed and it has thus been demonstrated that the rate of polymerization is a linear function of catalyst and monomer concentration. It has been proved that diffusion of monomer through a polymer layer is not the rate-controlling process. The effect of added oxygen on the reaction rate has been investigated and the reaction was found to have a small positive temperature coefficient. The molecular weights of the polymers as a function of reaction conditions were determined using a viscometric procedure. The results are interpreted in terms of a physical mechanism of catalyst coverage by polymer and by a kinetic scheme. A titanium species is shown to participate in an important termination process; no evidence for chain transfer processes was forthcoming. A number of mechanisms which are compatible with the observed kinetics are tentatively proposed.


2014 ◽  
Vol 481 ◽  
pp. 39-48 ◽  
Author(s):  
Siyang Tang ◽  
Zhen Liu ◽  
Xiaowei Yan ◽  
Ning Li ◽  
Ruihua Cheng ◽  
...  

2012 ◽  
Vol 476-478 ◽  
pp. 2188-2192
Author(s):  
Jian Cai ◽  
Tao Chen ◽  
Guo Zhen Wang ◽  
Jie Gao ◽  
Rui Ma ◽  
...  

An ionic liquid supported catalytic system, chloromethylimidazole acetylacetonate Cobolt(Ⅱ) was successfully used in the RATRP of methyl methacrylate. The chemical structure of obtained PMMA was confirmed by FT-IR and 1H NMR. The polymerization process in the presence of ionic liquid was thoroughly investigated. The results revealed that this kind of initiator and catalyst system could promote RATRP of MMA with the desired characteristics, and the RATRP proceeded in a controlled manner as evidenced by kinetic studies.


2004 ◽  
Vol 71 ◽  
pp. 1-14
Author(s):  
David Leys ◽  
Jaswir Basran ◽  
François Talfournier ◽  
Kamaldeep K. Chohan ◽  
Andrew W. Munro ◽  
...  

TMADH (trimethylamine dehydrogenase) is a complex iron-sulphur flavoprotein that forms a soluble electron-transfer complex with ETF (electron-transferring flavoprotein). The mechanism of electron transfer between TMADH and ETF has been studied using stopped-flow kinetic and mutagenesis methods, and more recently by X-ray crystallography. Potentiometric methods have also been used to identify key residues involved in the stabilization of the flavin radical semiquinone species in ETF. These studies have demonstrated a key role for 'conformational sampling' in the electron-transfer complex, facilitated by two-site contact of ETF with TMADH. Exploration of three-dimensional space in the complex allows the FAD of ETF to find conformations compatible with enhanced electronic coupling with the 4Fe-4S centre of TMADH. This mechanism of electron transfer provides for a more robust and accessible design principle for interprotein electron transfer compared with simpler models that invoke the collision of redox partners followed by electron transfer. The structure of the TMADH-ETF complex confirms the role of key residues in electron transfer and molecular assembly, originally suggested from detailed kinetic studies in wild-type and mutant complexes, and from molecular modelling.


1975 ◽  
Vol 14 (04) ◽  
pp. 330-338
Author(s):  
L. G. Colombetti ◽  
J. S. Arnold ◽  
W. E. Barnes

SummaryTc-99m pyridoxylidene glutamate has proven to be an excellent biliary scanning agent, far superior in many respect to the commonly used 1-131 rose bengal. The preparation of the compound as previously reported by Baker et al is too time consuming and requires the use of an autoclave which is not available in most nuclear medicine departments. In our facility, we have been preparing similar compounds using several aldehydes and monosodium glutamate to make labeled complexes having the same pharmacological characteristics. The mixture of monosodium glutamate, aldehyde, and Tc-99m pertechnetate is made slightly alkaline, purged with helium, and placed in a sealed vial. The vial, which is protected by a wire basket, is then heated in a laboratory oven at 130° C for a period of 15 to 20 minutes. During this time, the technetium is reduced to a lower valence state and bound to the complex formed. Chromatographic data show that these compounds are chemically similar to that previously reported. The compounds prepared concentrate in the gall bladder of the rabbit in less than 10 minutes. Kinetic studies have been performed on dogs with a scintillation camera and small digital computer to measure rates of blood clearance, liver and gall bladder uptake, and excretion into the intestine. The aldehyde — glutamate complex promises to be a useful scanning agent for the diagnosis of biliary and hepatocellular diseases.


1961 ◽  
Vol 05 (01) ◽  
pp. 001-020
Author(s):  
Douglas M. Surgenor ◽  
Nancy A. Wilson ◽  
Anne S. Henry

SummaryA method is described for the partial purification of a human plasma factor which accelerates the conversion of prothrombin to thrombin in the presence of tissue thromboplastin. This factor may be dried from the frozen state, and may be kept in stable dry form for long periods of time. The quantitative assay of this activity is done in a classical two-stage prothrombin system using tissue thromboplastin and calcium. From its properties, it is concluded that this activity corresponds to factor V, labile factor and plasma Ac-globulin.Chemical and kinetic studies reveal that human factor V is active in plasma and is destroyed by thrombin. Human serum has little or no factor V activity.These results thus fail to support the postulated activation of factor V during clotting. All of the kinetic data are consistent with an enzymatic role for factor V in the formation of tissue prothrombin activator (thromboplastin).


1979 ◽  
Vol 42 (05) ◽  
pp. 1473-1482 ◽  
Author(s):  
A Dup Heyns ◽  
P N Badenhorst ◽  
H Pieters ◽  
M G Lötter ◽  
P C Minnaar ◽  
...  

SummaryFactors influencing labelling of human platelets with 111Indium-8-hydroxyquinoline ([111In]-oxine) in a physiological saline medium were investigated. The efficiency of labelling is influenced by time of incubation, concentration of oxine, and pH of the incubating medium. It was found that a viable platelet population could be labelled under the following conditions: (1) centrifugation of platelet rich plasma in polystyrene conical tubes at 800 g for 15 min; (2) resuspension of the platelet pellet in saline, pH 5.5; (3) incubating for 30 min at 22°C with [111In]-oxine at a concentration of 6.25 mg oxine/litre platelet suspension; (4) washing once with platelet poor autologous plasma (PPP); and (5) finally resuspending the platelets in PPP. The labelled platelets aggregated normally with collagen and ADP. Electron microscopy, done immediately after labelling, showed internal organelle reorganization characteristic of activated platelets. These ultrastructural features were reversible on incubation in PPP at 37°C for 30 min. The 111In is not released from aggregated platelets and the label does not elute from incubated platelets for at least five hr. We conclude that human platelets thus labelled are suitable for in vivo kinetic studies.


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