Big Chemical Encyclopedia

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

Articles Figures Tables About

Myoglobin assay

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).
In contrast to the majority of CO-RMs in the literature CO-RM A1 does not contain any transition metals, but contains two sodium atoms. A previously reported myoglobin assay was used to assess if this compound could release CO, and several were performed at different pH to assess how this variable would affect CO release rates. [Pg.162]

CO-RM A1 was also used in an assay which employed amperometric electrodes to measure the amount of CO-released in solution at various pHs and temperatures. The performed assay is in agreement with the results of the myoglobin assays that were carried out. CO is released... [Pg.162]

Parent CO-RM 8 was the first pyrone compound to be tested in a myoglobin assay and it was unfortunately discovered that it did not release-CO in a myoglobin assay. This shows that this particular CO-RM is stable in aqueous solution and in the presence of myoglobin. It was not tested for co-release using irradiation but it is certainly possible that it could. [Pg.171]

CO-RM F8 was tested in the presence of a myoglobin assay and was found to release only 3 pM of CO in the presence of myoglobin without... [Pg.171]

Following massive crush injury, myoglobin released from damaged muscle fibers colors the urine dark red. Myoglobin can be detected in plasma following a myocardial infarction, but assay of serum enzymes (see Chapter 7) provides a more sensitive index of myocardial injury. [Pg.47]

Rota et al. [81,82] concluded that DCF fluorescence could not be a reliable assay of superoxide detection in cells because superoxide is formed during the DCFH oxidation by peroxidases. It has also been shown that DCFH is oxidized by heme, hemoglobin, myoglobin, and cytochrome c [83]. However, recent work by Caldefie-Chezet et al. [84] showed that the measurements of superoxide production by PMNs with the use of 2 -7 -dichlorofluorescin diacetate flow cytometry correlated with the data obtained by lucigenin- and luminol-amplified CL assays. [Pg.971]

Eu3+, Tb3+, Sm3+, Dy3+ complexes have different emission wavelengths with sharp peak profiles, which are suitable for multi-component immunoassay. Several Eu-Sm two-color time-resolved immunoassays have been reported. Since the sensitivity of Sm3+ chelates is not high compared to Eu3+ and Tb3+, Eu-Sm two-color assays are used for the simultaneous determination of a low concentration component (Eu) and a relatively high concentration component (Sm) in serum the assayed combinations are lutropin and follitropin, myoglobin and carbonic dehydratase, AFP and free (3-subunit of human chorionic gonadotrophin (Hemmila et al., 1987). Use of Eu-Tb is reported by Eriksson et al. (2000) for the simultaneous determination of human serum free and total PSA. [Pg.195]

Nephelometric methods in general are more sensitive than turbidimetric assays and have an average lower limit of detection of 0.1 to 10 mg/L for a serum protein. Lower detection limits are obtained in fluids, such as cerebrospinal fluid and urine, because of their lower lipid and protein concentrations, which results in a better signal-to-noise ratio. In addition, for low molecular weight proteins (e.g., myoglobin, MW 17,800), assay detection Emits can be lowered using a latex-enhanced procedure based on antibody-coated latex beads. ... [Pg.230]


See other pages where Myoglobin assay is mentioned: [Pg.1643]    [Pg.106]    [Pg.121]    [Pg.172]    [Pg.174]    [Pg.175]    [Pg.177]    [Pg.177]    [Pg.180]    [Pg.185]    [Pg.1643]    [Pg.106]    [Pg.121]    [Pg.172]    [Pg.174]    [Pg.175]    [Pg.177]    [Pg.177]    [Pg.180]    [Pg.185]    [Pg.704]    [Pg.129]    [Pg.31]    [Pg.310]    [Pg.970]    [Pg.471]    [Pg.373]    [Pg.344]    [Pg.608]    [Pg.69]    [Pg.28]    [Pg.31]    [Pg.10]    [Pg.43]    [Pg.276]    [Pg.704]    [Pg.12]    [Pg.169]    [Pg.194]    [Pg.237]    [Pg.171]    [Pg.164]    [Pg.1171]    [Pg.560]    [Pg.704]    [Pg.239]    [Pg.809]    [Pg.810]    [Pg.1653]   
See also in sourсe #XX -- [ Pg.175 , Pg.184 , Pg.187 , Pg.188 , Pg.189 ]




SEARCH



Myoglobin

© 2024 chempedia.info