The pyrolysis of di-t-butyl peroxide has been reinvestigated and used as a source of methyl radicals to study the abstraction reaction between methyl radicals and formaldehyde. At low [HCHO]/[peroxide] ratios the system was simple enough for kinetic analysis, and a value of 6.6 kcal/mole was obtained for the activation energy. At higher [HCHO]/[peroxide] ratios the system became very complicated, possibly due to the increased importance of addition reactions.
SummaryApplication of the methods of enzyme-kinetic analysis to the results of clotting tests is feasible and can yield useful results. However, the standard methods of enzyme kinetics are not applicable without modifications imposed by the peculiarities of the blood-clotting enzyme system. The influence of the following complicating circumstances is calculated :1. Substrate is not present in excess.2. Only relative measures exist for concentrations of substrate or enzymes.3. Enzymes and substrates are often added together.4. Reagents are not pure.5. Clotting-time is our only measure for clotting-velocity.Formulas are deduced, which makes it possible to recognize the effect of these complications.
The Addition Reactions of Ethanol to Ethylene Induced by Gamma-ray Irradiation in the Gaseous Phase. II. A Kinetic Analysis of the Results