Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Proteomes kinetic changes

Example of Use Identification of Kinetic Proteome Changes upon Ligand Activation of Trk-Receptors... [Pg.40]

Enzymes may be measured by monitoring a reduction in substrate concentration or an increase of reaction product. The majority of the common enzymes can be measured using a kinetic approach in which the velocity of the enzyme reaction is monitored by serial measurements over a short time period. For some enzymes, the measurement reactions are linked to the enzyme cofactors nicotinamide adenine dinucleotide (NAD) or nicotinamide dinucleotide phosphate (NADP), and changes in these cofactors are measured in the ultraviolet spectrum. Reactions can be linked through second- or third-step reactions where these cofactors are involved (e.g., for AST and ALT). Other enzymes may be measured colorimetrically (e.g., ALP and GGT). Very few enzymes have been measured as enzyme mass, although proteomic methods may lead to greater utilization of enzyme mass measurements. [Pg.23]


See other pages where Proteomes kinetic changes is mentioned: [Pg.24]    [Pg.29]    [Pg.451]    [Pg.161]    [Pg.33]    [Pg.224]    [Pg.34]    [Pg.40]    [Pg.883]    [Pg.402]    [Pg.1714]    [Pg.207]    [Pg.2878]    [Pg.33]    [Pg.312]    [Pg.320]    [Pg.375]    [Pg.170]    [Pg.125]   
See also in sourсe #XX -- [ Pg.13 , Pg.39 ]




SEARCH



© 2024 chempedia.info