Relevant bibliographies by topics / Myoglobin Assay

Academic literature on the topic 'Myoglobin Assay'

Author: Grafiati
Published: 10 March 2023

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Journal articles on the topic "Myoglobin Assay"

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Massoubre, Catherine, Laurent Chivot, Francine Mainard, Boumediene Bridji, and Yves Madec. "Immunonephelometric assay of myoglobin." Clinica Chimica Acta 201, no. 3 (September 1991): 223–29. http://dx.doi.org/10.1016/0009-8981(91)90373-k.

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Delanghe, J. R., J. P. Chapelle, and S. C. Vanderschueren. "Quantitative nephelometric assay for determining myoglobin evaluated." Clinical Chemistry 36, no. 9 (September 1, 1990): 1675–78. http://dx.doi.org/10.1093/clinchem/36.9.1675.

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Abstract A recently introduced automated nephelometric immunoassay involving shell/core particles for determination of myoglobin (Behringwerke) was evaluated with the BNA Nephelometer. Method precision was good: the intra-assay CV varied between 1.5% and 6.1%; with daily calibration, the interassay CV ranged between 1.5% and 7.5%. For usual sample dilutions, the assay response varied linearly with myoglobin concentrations up to 23.1 nmol/L. After automatic dilution by the instrument, concentrations up to 2310 nmol/L could be measured without high-dose "hook" effect. Further manual dilution allowed measurement of myoglobin concentrations up to 26,000 nmol/L. Calibration was stable for at least seven days. We detected no significant interferences from hemoglobin, haptoglobin, bilirubin, iodine-containing contrast media, and rheumatoid factors. Treating lipemic samples with Lipoclean (Behringwerke) decreased test results. Simultaneously drawn serum and plasma samples from the same subject showed no consistent differences in myoglobin concentrations. The mean reference myoglobin concentration was 1.380 (SD 0.82) nmol/L for men and 0.878 (SD 0.45) nmol/L for women. In patients with renal insufficiency, serum creatinine values were moderately related to serum myoglobin values (r = 0.465). Although a commercial radioimmunoassay (Byk-Sangtec) and the nephelometric assay intercorrelated well (r = 0.929), values obtained by nephelometry were significantly lower (P less than 0.05). By both assays, results for heart and skeletal muscle tissue extracts showed no correlation, a finding that suggests the existence of multiple forms of myoglobin in human tissues. We conclude that immunonephelometry is a rapid, practical, and reliable method for measuring myoglobin in serum.
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Gülcü, Özgehan Cansu, and Elvan Üstün. "A simple theoretical approach to converging of Myoglobin-Assay with different pH values." Acta Chimica Slovaca 14, no. 1 (January 1, 2021): 97–104. http://dx.doi.org/10.2478/acs-2021-0012.

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Abstract Many metal carbonyl complexes have been synthesized and analyzed as CO-releasing agents. As in many bioactivity assays, differences between in-vitro and in-vivo studies in Myoglobin Assay have been observed. Adjustment of in-vitro conditions to in-vivo conditions is one way to overcoming this problem. Changing the conditions of each in-vivo assay is not possible considering the available grant, material, and labor facilities. In-silico methods are suitable as they provide better in-vitro conditions before experimental procedures. A method which is easy to employ on a basic computer could be more suitable to observe the assay convergence. In this study, global reactivity descriptors were used as an approach to investigate pH differences in myoglobin assay. Global reactivity descriptors of the molecules were compared with myoglobin assay results at different pH values and molecular docking results performed with optimized molecules in different solvents. The following complexes were studied: [Mn(CO)3(bpy)(L)]PF6 (bpy: 2,2-bipyridyl, L: benzylbenzimidazole, 4-chlorobenzylbenzimidazole).
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Vuletich, Jennifer L., and Yoichi Osawa. "Chemiluminescence Assay for Oxidatively Modified Myoglobin." Analytical Biochemistry 265, no. 2 (December 1998): 375–80. http://dx.doi.org/10.1006/abio.1998.2926.

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Delanghe, J., J. P. Chapelle, M. El Allaf, and M. De Buyzere. "Quantitative Turbidimetric Assay for Determining Myoglobin Evaluated." Annals of Clinical Biochemistry: An international journal of biochemistry and laboratory medicine 28, no. 5 (September 1, 1991): 474–79. http://dx.doi.org/10.1177/000456329102800509.

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Pagani, Franca, Roberto Bonora, Graziella Bonetti, and Mauro Panteghini. "Evaluation of a sandwich enzyme-linked immunosorbent assay for the measurement of serum heart fatty acid-binding protein." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 39, no. 4 (July 1, 2002): 404–5. http://dx.doi.org/10.1258/000456302760042173.

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Background: We evaluated the sandwich enzyme-linked immunosorbent assay (ELISA) MARKIT®-M for the determination of heart fatty-acid-binding protein (H-FABP). Results and Conclusions: The between-run coefficient of variation of this assay was <3·9 and it showed good correlation with a previously established ELISA method. The upper reference limit in 30 healthy individuals was 6·1 μg/L. Admission serum H-FABP was evaluated against myoglobin in 41 patients with suspected myocardial infarction (onset of symptoms ≤ 5 h). H-FABP showed the same diagnostic efficiency as myoglobin [area (standard error) under the receiver operating characteristic curve: 0·798 (0·079) for H-FABP, 0·771 (0·085) for myoglobin, P = 0·55]. However, using the upper reference limit as decision cut-off, the sensitivity for H-FABP [91%; 95% confidence interval (CI): 76-98%] was significantly ( P = 0·019) higher than that of myoglobin (65%; 95% CI: 47-80%).
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Liebetrau, Christoph, Helge Möllmann, Holger Nef, Sebastian Szardien, Johannes Rixe, Christian Troidl, Matthias Willmer, et al. "Release Kinetics of Cardiac Biomarkers in Patients Undergoing Transcoronary Ablation of Septal Hypertrophy." Clinical Chemistry 58, no. 6 (June 1, 2012): 1049–54. http://dx.doi.org/10.1373/clinchem.2011.178129.

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Abstract BACKGROUND The release kinetics of cardiac troponin T measured with conventional vs high-sensitivity cardiac troponin T (hs-cTnT) assays in patients with acute myocardial infarction (AMI) is difficult to establish. METHODS We analyzed the release kinetics of cTnT measured by fourth generation and high-sensitivity assays, creatine kinase-MB (CK-MB), and myoglobin in patients with hypertrophic obstructive cardiomyopathy undergoing transcoronary ablation of septal hypertrophy (TASH), a model of AMI. Consecutive patients (n = 21) undergoing TASH were included. Serum and EDTA-plasma samples were collected before and at 15, 30, 45, 60, 75, 90, and 105 min, and 2, 4, 8, and 24 h after TASH. RESULTS cTnT concentrations measured by the hs assay were significantly increased at 15 min [21.4 ng/L, interquartile range (IQR) 13.3–39.7 ng/L vs 11.3 ng/L, IQR 6.0–18.8 ng/L at baseline; P = 0.031]. In comparison, cTnT concentrations measured by the conventional fourth generation assay increased significantly at 60 min (30.0 ng/L, IQR 20.0–30.0 ng/L vs &lt;10.0 ng/L, IQR &lt;10.0–10.0 ng/L; P &lt; 0.01), CK-MB at 90 min (8.4 μg/L, IQR 6.9–14.4 μg/L vs 0.9 μg/L, IQR 0.4–1.1 μg/L; P &lt; 0.01), and myoglobin at 30 min (188.0 μg/L, IQR 154.0–233.0 μg/L vs 38.0 μg/L, IQR 28.0–56.0; P &lt; 0.01). CONCLUSIONS cTnT concentrations measured by the hs assay were significantly increased after TASH at all of the time points, with a doubling at 15 min after induction of AMI, confirming earlier evidence of myocardial injury compared to the fourth generation cTnT assay and CK-MB and myoglobin.
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Zaninotto, Martina, Franca Pagani, Sara Altinier, Paolo Amboni, Roberto Bonora, Alberto Dolci, Patrizia Pergolini, Arialdo Vernocchi, Mario Plebani, and Mauro Panteghini. "Multicenter Evaluation of Five Assays for Myoglobin Determination." Clinical Chemistry 46, no. 10 (October 1, 2000): 1631–37. http://dx.doi.org/10.1093/clinchem/46.10.1631.

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Abstract Background: Lacking assay standardization, different myoglobin methods may produce results that differ significantly. Methods: A multicenter study was carried out to compare the analytical performance of five commercially available assays for myoglobin measurement. Linearity, imprecision, interferences, and method comparison were studied according to NCCLS guidelines, whereas reference values were determined following IFCC recommendations. Results: The BNA and Opus showed relatively high imprecision (all but one total CV &gt;7.4%). Other assays showed lower CVs, but they varied among laboratories, particularly at a normal myoglobin concentration (Access, 6.0–11%; Hitachi, 3.8–5.8%; Stratus, 3.4–6.5%). Results were lower in anticoagulated samples on the Access, in heparin and citrate samples on the Stratus, and in citrate samples on the BNA and Opus, and increased in heparin and EDTA samples on the Hitachi. Use of separator gel produced results significantly lower (P &lt;0.001) on the Hitachi and higher (P = 0.016) on the Opus. Bilirubin, turbidity, and hemoglobin had no effect on evaluated methods, but rheumatoid factor affected the Access. In method comparisons, high correlation coefficients (≥0.98) were obtained. The Stratus gave higher results; however, the Access and BNA gave the lowest. The following upper reference limits (μg/L) for men and women, respectively, were obtained: Access, 70 and 52; BNA, 51 and 49; Hitachi, 67 and 58; Opus, 80 and 50; and Stratus, 86 and 63. Conclusion: The possibility of high imprecision and marked disagreement among commercial myoglobin assays should be carefully considered in clinical practice.
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Kumar, Udit, Shilpa Jose, Dhanaraj Divya, Pitchavel Vidhyapriya, Natarajan Sakthivel, and Bala Manimaran. "Self-assembly of manganese(i) based thiolato bridged dinuclear metallacycles: synthesis, characterization, cytotoxicity evaluation and CO-releasing studies." New Journal of Chemistry 43, no. 19 (2019): 7520–31. http://dx.doi.org/10.1039/c8nj06271d.

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Marques, Sara S., Luís M. Magalhães, Ana I. P. Mota, Tânia R. P. Soares, Barbara Korsak, Salette Reis, and Marcela A. Segundo. "Myoglobin microplate assay to evaluate prevention of protein peroxidation." Journal of Pharmaceutical and Biomedical Analysis 114 (October 2015): 305–11. http://dx.doi.org/10.1016/j.jpba.2015.06.006.

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Dissertations / Theses on the topic "Myoglobin Assay"

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Magalhães, Luís Miguel Andrade de. "Myoglobin microplate assay to evaluate prevention of protein peroxidation." Master's thesis, 2016. https://repositorio-aberto.up.pt/handle/10216/89504.

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Magalhães, Luís Miguel Andrade de. "Myoglobin microplate assay to evaluate prevention of protein peroxidation." Dissertação, 2016. https://repositorio-aberto.up.pt/handle/10216/89504.

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Berrino, Emanuela, Claudiu Supuran, Alessandro Mugelli, and Fabrizio Carta. "Carbonic Anhydrase Inhibitors: Versatile Agents for the Treatment of Human Diseases." Doctoral thesis, 2020. http://hdl.handle.net/2158/1188882.

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The Carbonic Anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes expressed in almost all living organisms. Being one of the main actors in pH regulation and in the maintenance of proper concentrations of CO2, the dysruption of the activity of such enzymes, by means of adequate modulators, is a validated strategy for the treatment of human affecting pathologies and for the eradication of etiological agents (i.e. pathogenic bacteria, fungi and protozoa). In addition, CA-based biotechnological applications (i.e. CO2 capture) may benefit from modulation of the enzymatic activity. CA Inhibitors (CAIs) have been extensively investigated over the time, and have been validated for the management of hypertensive glaucoma, systemic hypertension, epilepsy, obesity related diseases and recently neuropathic pain, inflammation and hypoxic tumors. Although CA activators (CAA) traditionally lacked interests, currently a repurposing of such compounds is underway with promising results as potential agents for the management of memory deficits related to neurodegenerative diseases. In this Thesis work, an introductive overview on CAs as the main biological targets (Chapter 1) and three distinctive projets (Chapters 2-4) are reported ranging from synthetic chemistry to enzyme biology and spctrophotometry. The first one (Chapter 2) concerns the synthesis and evaluation of new CAIs with Carbon Monoxide (CO) releasing properties for the management of RA. The reported compounds have been fully characterized, their CA inhibitory properties along with the CO releasing effect were assessed. In particular, a spectrophotometric assay was properly set with slight modifications of the protocols reported in the literature. This allowed to obtain a precise and quantitative evaluation of CO released over time from our compounds. The pain refief effect of the designed CAI-CORMs was also evaluated in a rat model of RA with very promising results. The second project (Chapter 3) was aimed to synthetize a small series of CAI-AZT hybrids and to evaluate them as Telomerase Inhibitors, thus with possible antitumoral applications. The compounds synthetized have been profiled in vitro on seven CA isoforms (i.e. I, II, Va, VB, VII, IX and XII). The effects of our compounds on Telomerase Activity have been also determined showing a low-medium inhibition potency. Two promising derivatives have been identified with good IC50 and IC90 values. Co-crystallyzation of selected compounds in adduct with hCA II has been performed and their binding modes were determined. The third project (Chapter 4) was entirely carried out during my six-months visiting student experience at the University of Poitiers in France, and it concerns the synthesis in Superacid medium of new mono and di-fluorinated diamines as CAIs. Insertion of one or more C-F bonds is a validated strategy in Medicinal Chemistry. Fluorine insertion can modulate pharmacokinetic and pharmacodynamic properties of the compounds, thus being an attractive tool in the design of bioactive compounds. Another unrelated project included in this Chapter, is the synthesis of enantiopure fluorinated tricyclic scaffolds obtained by means of a diastereoselective approach.
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Book chapters on the topic "Myoglobin Assay"

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Taniguchi, Yoshihiro, and Naohiro Takeda. "High-Pressure FTIR Studies of the Secondary Structure of Proteins." In High Pressure Effects in Molecular Biophysics and Enzymology. Oxford University Press, 1996. http://dx.doi.org/10.1093/oso/9780195097221.003.0010.

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Infrared spectra of five globular proteins (bovine pancreas ribonuclease A, horse skeletal muscle myoglobin, bovine pancreas insulin, horse heart cytochrome c, egg white lysozyme) in 5% D2O solutions (pD 7.0) were measured as a function of pressure up to 1470 MPa at 30 °C. According to the second-derivative spectral changes in the observed amide I band of the proteins, which indicate that the α-helix and β-sheet substructures of the secondary structures break dramatically into the random coil conformation, ribonuclease A and myoglobin are denatured reversibly at 850 MPa and 350 MPa, respectively. Lysozyme denatures partially and reversibly at 670 MPa, as shown by decrease in the α-helix and β-turn substructures, but no change occurs in the random coil and β-sheet substructures. The secondary structure of cytochrome c is not disrupted at pressures up to 1470 MPa, and partial transformation of the α-helix of insulin to random coil starts at 960 MPa. Hydrogen-deuterium exchange of protons on the amide groups in the protein interior is increased by external pressure and is associated with the pressure-induced protein conformational changes. A number of studies on the effects of pressure on protein denaturation have been carried out using various high-pressure detection methods: ultraviolet absorbance spectroscopy (Brandts et al., 1970; Hawley, 1971), visible absorbance spectroscopy (Zipp & Kauzmann, 1973), fluorescence intensity spectroscopy (Li et al., 1976), polarization fluorescence spectroscopy (Chryssomallis et al., 1981), and enzyme activity assays (Taniguchi & Suzuki, 1983; Makimoto et al., 1989). These techniques have the great advantage of being applicable to pressure-induced reversible denaturation of proteins to identify the thermodynamic parameters, especially the volume change and compressibility of a protein in solution, because the experiments can be run under dilute conditions at a protein concentration of less than 0.05% w/v. Therefore, these data reflect the intramolecular phenomena of reversible pressure changes and provide the volume changes accompanying the denaturation of proteins, which are due to the difference in partial molal (specific) volume between the native and denatured proteins in solution.
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