China
Africa
Explore chapters and articles related to this topic
Preparation and Health Benefits of Rice Beverages From Ethnomedicinal Plants: Case Study in North-East of India
Published in Megh R. Goyal, Arijit Nath, Rasul Hafiz Ansar Suleria, Plant-Based Functional Foods and Phytochemicals, 2021
Vedant Vikrom Borah, Mahua Gupta Choudhury, Probin Phanjom
Biuret test is used as a standard method for the qualitative detection of protein in rice beer. Bovine serum albumin is used as a standard in Biuret test [13, 39, 40]. Reports suggest the presence of protein with concentration of 0.97 mgmL−1 in judima [39], 1.05 mgmL−1 in poro apong [40], 9.63-12.42 mgmL−1 in rice beer prepared by tribes in Tripura [13], 3.2 mgmL−1 in boro, 5.7 mgmL−1 in poro, 4.2 mgmL−1 in judima and 6.2 mgmL−1 in jumai [43].
Assay of Antibiotics in Mammalian Cell Culture
Published in Adorjan Aszalos, Modern Analysis of Antibiotics, 2020
Add 5 ml of solution C to all assay tubes. Incubate at 37°C for 1 hr or heat to 56—60°C for 5 min to dissolve the cell material. Shake for 5—15 min on a reciprocal shaker to complete the dissolution of cells. The intensity of the biuret color produced by the alkaline copper sulfate tartrate (solution C) with the protein is an indication of the amount of protein solution that can be used to react with the Folin-Ciocalteau reagent to produce a reading within the range of the spectrophotometer. Appropriate dilutions of cell solutions showing a pale to deep violet color should be made and further diluted with solution C to a final volume of 5 ml as outlined in the table:
A Neurochemical Approach to Elucidate Metabotropic vs. Ionotropic Glutamate Receptor Activities in Rat Hippocampal Slices
Published in Avital Schurr, Benjamin M. Rigor, BRAIN SLICES in BASIC and CLINICAL RESEARCH, 2020
Darryle D. Schoepp, Manisha A. Desai
Isolation of 3H-inositol monophosphates (3H-IPs) is performed by anion exchange liquid chromatography.61 QMA Sep-Pak cartridges (Millipore Corporation, Milford, MA) are prepared by washing in 10 ml of water, 8 ml of 1.0 M triethylammonium hydrogen carbonate (TEAB, available from Fluka BioChemika, Buchs, Switzerland), and then 10 ml of water. After centrifugation of the homogenate, the supernatant containing water-soluble 3H-inositol phosphates is passed over a QMA Sep-Pak cartridge on an Amersham Super Separator-24 apparatus. The column is washed with 10 ml of water, followed by 4 ml of 0.02 M TEAB solution, to remove 3H-inositol precursor. 3H-IPs are eluted into large glass scintillation vials using 4 ml of 0.1 M TEAB. Scintillation cocktail is added to each vial for counting. Tissue pellets are analyzed for total protein using the Biuret method.62 The data are expressed at DPM 3H-IPs/mg of protein or percent of the basal hydrolysis value in each experiment. This procedure results in constant basal hydrolysis and a linear agonist-induced increase in 3H-inositol monophosphate formation over the course of the 60-min hydrolysis incubation in brain slices.63
Potential interference of in vitro carbamylation on C-reactive protein laboratory measurement
Published in Scandinavian Journal of Clinical and Laboratory Investigation, 2023
Carolina dos Santos Stein, José Pedro Etchepare Cassol, Rafael Noal Moresco
CRP concentrations were measured by immunoturbidimetric assay, and total protein was determined using biuret or pyrogallol red (Bioclin, Belo Horizonte, MG, Brazil) colorimetric methods. Following the manufacturer’s instructions, these analyses were performed using a BS 380® automated analyzer (Mindray, Shenzhen, China). For CRP quantification, 3 µL of the sample was pipetted into the reaction cuvette with 240 µL of the buffer reagent and 60 µL of the latex sensitized with anti-CRP antibodies. The mixture was incubated for 8 min and measured at 546 nm. The total protein concentrations in the samples of CRP standard solution were measured using the pyrogallol red assay. Briefly, 4 µL of the sample was pipetted into the reaction cuvette with 200 µL of the color reagent. The mixture was incubated for 6 min and measured at 605 nm. The biuret method was used to quantify total proteins in serum pools: 4 µL of the sample was pipetted into the reaction cuvette with 200 µL of the color reagent. The mixture was incubated for 7 min and measured at 564 nm. Carbamylation was characterized using the OxiSelect™ Protein Carbamylation Sandwich ELISA Kit (Catalog Number STA-877, Cell Biolabs, San Diego, CA, USA) following the manufacturer’s instructions. After all incubations, the microplate was read in the FilterMax F3 Multi-Mode Microplate Reader (Molecular Devices, San Jose, CA, USA). This assay measures the formation of carbamyl-lysine during the carbamylation of proteins. The detection sensitivity limit is 1.5 ng/mL.
Ameliorative effects of hexane extract of Garcinia kola seeds Heckel (Clusiaceae) in cisplatin-induced hepatorenal toxicity in mice
Published in Drug and Chemical Toxicology, 2022
Adeniyi Folayan, Emmanuel Akani, Olayinka A. Adebayo, Olubukola O. Akanni, Solomon E. Owumi, Abiola S. Tijani, Oluwatosin A. Adaramoye
The concentration of protein in the sample was assessed by the technique of Gornal and David (1949) using Biuret reagent. Albumin and creatinine levels were evaluated by the methods of Doumas and Biggs (1971) and Bartels et al. (1972), respectively. Serum urea and bilirubin levels were assessed by the process of Fawcett and Scott (1960) and Jendrassik (1938), respectively. The activities of alanine and aspartate aminotransferases were assessed by the methods of Mohun and Cook (1957) and Reitman and Frankel (1957) The activities of superoxide dismutase and catalase were evaluated by the techniques of Misra and Fridovich (1972), and Clairborne (1995), respectively. The level of reduced glutathione was assessed as described by Beutler et al. (1963) The activity of glutathione peroxidase was evaluated by the technique of Rotruck et al. (1973).
The influence of erdosteine administration on lead-induced oxidative stress in rat muscle
Published in Drug and Chemical Toxicology, 2022
Michał Dobrakowski, Anna Machoń-Grecka, Przemysław Nowak, Patrycja Szczęsny, Maciej Maciejczyk, Aleksandra Kasperczyk, Tomasz Pryzwan, Sławomir Kasperczyk
The level of protein was measured by the biuret method by Richterich (1971). The method of Oyanagui (1984) was used to measure the activity of SOD. The activities of Mn-SOD and CuZn-SOD isoenzymes were measured using potassium cyanide as the inhibitor of the CuZn-SOD activity. The activity of SOD was expressed in nitric units (NU). The activity of SOD is equal to 1 NU when it inhibits nitric ion production by 50%. Activities of SOD were normalized to mg of protein (NU/mg protein). The CAT activity was measured by the Aebi (1984) kinetic method and was expressed in international units per mg of protein (IU/mg protein). The glutathione peroxidase (GPx) activity was measured by the kinetic method of Paglia and Valentine (1967) and was expressed as µmol of NADPH oxidized per minute per g of hemoglobin (U/g Hb). The activity of glutathione reductase (GR) was measured by the method of Richterich (1971) and expressed as µmol of NADPH utilized per minute normalized to g of protein (IU/g P). The activity of glutathione-S-transferase (GST) was measured according to the kinetic method of Habig and Jakoby (1981). The activity of GST was expressed as µmol of thioether produced per minute normalized to g of protein (IU/g P). The level of malondialdehyde (MDA) was determined by the method of Ohkawa et al. (1979). The results were recorded as mmol per 100 mg of muscle tissue (µmol/100 mg T).