Search results
Results From The WOW.Com Content Network
1-Aminopentane is an organic compound with the formula CH 3 (CH 2) 4 NH 2. It is used as a solvent , as a raw material in the manufacture of a variety of other compounds, including dyes, emulsifiers , and pharmaceutical products, [ 1 ] and as a flavoring agent .
The Michaelis constant has units of concentration, and for a given reaction is equal to the concentration of substrate at which the reaction rate is half of . [6] Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions.
An ion gradient has potential energy and can be used to power chemical reactions when the ions pass through a channel (red). Hydrogen ions, or protons, will diffuse from a region of high proton concentration to a region of lower proton concentration, and an electrochemical concentration gradient of protons across a membrane can be harnessed to ...
The iodine clock reaction is a classical chemical clock demonstration experiment to display chemical kinetics in action; it was discovered by Hans Heinrich Landolt in 1886. [1] The iodine clock reaction exists in several variations, which each involve iodine species ( iodide ion, free iodine, or iodate ion) and redox reagents in the presence of ...
Aminopentane may refer to: 1-Aminopentane; 2-Aminopentane; 3-Aminopentane This page was last edited on 4 August 2019, at 16:05 (UTC). Text is available under the ...
α-Propylphenethylamine (APPEA or α-Pr-PEA), also known as 1-phenyl-2-aminopentane, is a stimulant drug of the phenethylamine and amphetamine families. [1] [2] It is the analogue of the β-phenethylamine (PEA) derivatives amphetamine (α-methylphenethylamine; "AMPEA") and phenylisobutylamine (α-ethylphenethylamine; AEPEA) in which the α-alkyl chain has been further lengthened to be a propyl ...
The substrate concentration midway between these two limiting cases is denoted by K M. Thus, K M is the substrate concentration at which the reaction velocity is half of the maximum velocity. [2] The two important properties of enzyme kinetics are how easily the enzyme can be saturated with a substrate, and the maximum rate it can achieve.
The bistartratocuprate(II) complex oxidizes the aldehyde to a carboxylate anion, and in the process the copper(II) ions of the complex are reduced to copper(I) ions. Red copper(I) oxide then precipitates out of the reaction mixture, which indicates a positive result i.e. that redox has taken place (this is the same positive result as with ...