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Myoglobin light absorption

The absorption coefficient of myoglobin at 580 nm is 15,000 M cm f What is the absorbance of a 1 mg ml solution across a 1-cm path What percentage of the incident light is transmitted by this solution ... [Pg.188]

Development of electrophoretic protein separation techniques have been paralleled by improvements in protein detection methods. Protein detection in early electrophoretic applications, utilizing electrophoretic separations of solutions or colloidal suspensions from about 1816 to 1937, was limited to direct visualization of proteins coated onto microspheres, or studies of naturally colored proteins such as hemoglobin, myoglobin, or ferritin <1-4). An increase in sensitivity and the ability to detect non-colored proteins was achieved by the use of the specific absorption, by proteins, of ultraviolet light. This detection technique permitted Tiselius,in 1937, to demonstrate the quantitative electrophoretic separation of ovalbumin, serum globulin fractions and Bence Jones proteins (S). Tiselius also employed the shadows, or schlieren, created by the boundaries, due to the different concentrations of proteins in the electrophoretic system to detect protein position and concentration ( ). These detection methods served as the main methods for protein detection in the liquid electrophoresis systems. However,... [Pg.74]

Figure 11 Schematic highlighting myoglobin assay used to confirm NO photorelease from the Ru-pHEMA hydrogel. The Inset displays the absorption spectra of Mb (red (light gray in the print version) trace), reduced Mb (green (light gray in the print version) trace), and Mb-NO (blue trace (light gray in the print version), Soret band at 420 nm). Figure 11 Schematic highlighting myoglobin assay used to confirm NO photorelease from the Ru-pHEMA hydrogel. The Inset displays the absorption spectra of Mb (red (light gray in the print version) trace), reduced Mb (green (light gray in the print version) trace), and Mb-NO (blue trace (light gray in the print version), Soret band at 420 nm).
Laser flash photolysis is often used to measure the binding rate of CO to heme proteins, such as myoglobin (Mb), because CO dissociates from the bound state relatively easily on absorption of energy from an intense and short pulse of light. The reaction is usually run under pseudo-first-order conditions. For a reaction in which [Mb]o = 10 mmol dm" , [CO] = 400 mmol dm" , and the rate constant is 5.8 X 10 dm mol" s" , plot a curve of [Mb] against time. The observed reaction is Mb + CO —> MbCO. [Pg.240]


See other pages where Myoglobin light absorption is mentioned: [Pg.910]    [Pg.103]    [Pg.4]    [Pg.494]    [Pg.152]    [Pg.574]    [Pg.951]    [Pg.694]    [Pg.358]    [Pg.591]    [Pg.358]    [Pg.120]    [Pg.49]    [Pg.694]    [Pg.38]    [Pg.647]    [Pg.314]    [Pg.230]    [Pg.225]   
See also in sourсe #XX -- [ Pg.574 , Pg.575 ]




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