Journal articles: 'Bradford assay'

1

Harlow, E., and D. Lane. "Bradford Assay." Cold Spring Harbor Protocols 2006, no. 6 (November 1, 2006): pdb.prot4644. http://dx.doi.org/10.1101/pdb.prot4644.

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Kielkopf, Clara L., William Bauer, and Ina L. Urbatsch. "Bradford Assay for Determining Protein Concentration." Cold Spring Harbor Protocols 2020, no. 4 (April 2020): pdb.prot102269. http://dx.doi.org/10.1101/pdb.prot102269.

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Zuo, Shu-Sheng, and Per Lundahl. "A Micro-Bradford Membrane Protein Assay." Analytical Biochemistry 284, no. 1 (August 2000): 162–64. http://dx.doi.org/10.1006/abio.2000.4676.

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Jones, Clive G., J. Daniel Hare, and Steve J. Compton. "Measuring plant protein with the Bradford assay." Journal of Chemical Ecology 15, no. 3 (March 1989): 979–92. http://dx.doi.org/10.1007/bf01015193.

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Pohanka, Miroslav, and Vitezslav Vlcek. "Immunoassay of Glomalin by Quartz Crystal Microbalance Biosensor Containing Iron Oxide Nanoparticles." International Journal of Analytical Chemistry 2020 (September 1, 2020): 1–6. http://dx.doi.org/10.1155/2020/8844151.

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Glomalin is a soil protein resembling heat shock protein (HSP) 60 and exerting high affinity to metals, causing retention of water in the environment and improving mechanical stability of soil. Currently, glomalin is determined in the soil or other samples by combination of autoclaving extraction and total protein determination typically by the Bradford method. In this paper, a piezoelectric biosensor was prepared to determine glomalin in a label-free measurement. The biosensor contained antibodies immobilized on quartz crystal microbalance (QCM), and the recognition layer was stabilized by iron oxide nanoparticles. The assay was tested on real soil samples and compared with the standard Bradford assay. Limit of detection of the assay was equal to 2.4 µg/g for a soil extract with a volume of 50 µl. The assay takes approximately half of an hour and was fully correlated to the Bradford assay. The biosensor had significant advantages than the other methods: it worked in a label-free mode and was fully applicable for practical samples.

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Belitsky, Jason M., Alshakim Nelson, and J. Fraser Stoddart. "Monitoring cyclodextrin–polyviologen pseudopolyrotaxanes with the Bradford assay." Org. Biomol. Chem. 4, no. 2 (2006): 250–56. http://dx.doi.org/10.1039/b509576j.

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López, JoséManuel, Santiago Imperial, Rodrigo Valderrama, and Salvador Navarro. "An improved bradford protein assay for collagen proteins." Clinica Chimica Acta 220, no. 1 (October 1993): 91–100. http://dx.doi.org/10.1016/0009-8981(93)90009-s.

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Gunasekaran, Baskaran, Mohd Hakimi Mohd Kasim, Shamala Salvamani, and M. Y. Shukor. "Field trials on heavy metals using alpha-chymotryopsin enzyme assay." Journal of Environmental Microbiology and Toxicology 2, no. 1 (July 29, 2014): 25–34. http://dx.doi.org/10.54987/jemat.v2i1.90.

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An inhibitive enzyme assay using Î±-chymotrypsin was developed. This serine protease was assayed using Bradford-protease casein assay system. This assay is sensitive to several metals such as mercury Hg2+, Zn2+, and Cr6+. The IC50 (concentration of toxicant giving 50% inhibition) of Hg2+, Zn2+, and Cr6+ is 1.34 mg/l, 2.49 mg/l and 2.19 mg/l respectively. The principle of the protein assay using casein as a substrate relies upon the inability of the Bradford dye to stain polypeptide with less than a molecular weight of 2 kDa. In the presence of heavy metals that can inhibit this enzyme, casein is not being degraded and it is stained by the Bradford dye reagent giving a blue colour. On the other hand, in the absence of inhibitors, casein is hydrolyzed to polypeptides with molecular weight of 2 kDa and below which canâ€™t be stained by Bradford dye-binding reagent. Therefore, solution remains brown in colour. The synergistic effect of combined heavy metals was studied and the results obtained shown that there were elevation of percentage of inhibition several folds. The combination of Hg2+ (0.3 mg/l) with Zn2+ (0.8 mg/l), Hg2+ (0.3 mg/l) with Cr6+ (1.8 mg/l), Zn2+ (0.8 mg/l) with Cr6+ (1.8 mg/l) increased 15.6, 73.0, 78.8 % respectively. Biomonitoring of heavy metals using an inhibitive Î±-chymotripsin assay was carried out. There sites for biomonitoring were Prai Industrial Areas, Bukit Tengah Industrial Area, Juru Industrial Area, Melaka River, Kuyoh River and Endau Rompin National Park. Many of the samples gave positive inhibitory effect on this enzyme. Those samples were analysed by inductively coupled plasma-optical emission spectrometry (ICP-OES) for confirmation of the presence of heavy metals that inhibited this enzyme.

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Braunstein, J. D., and M. Halwer. "Bradford protein assay and determination of estrogen and progesterone receptors." Clinical Chemistry 32, no. 8 (August 1, 1986): 1588–89. http://dx.doi.org/10.1093/clinchem/32.8.1588b.

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Gotham, Simon M., Peter J. Fryer, and William R. Paterson. "The measurement of insoluble proteins using a modified Bradford assay." Analytical Biochemistry 173, no. 2 (September 1988): 353–58. http://dx.doi.org/10.1016/0003-2697(88)90199-6.

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Rekowski, Azin, Georg Langenkämper, Markus Dier, Monika A. Wimmer, Katharina A. Scherf, and Christian Zörb. "Determination of soluble wheat protein fractions using the Bradford assay." Cereal Chemistry 98, no. 5 (May 30, 2021): 1059–65. http://dx.doi.org/10.1002/cche.10447.

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Jiang, Chen, Luo Hao, Tao Mei, Liu Zhongchuan, and Wang Ganggang. "Quantitation of nucleoprotein complexes by UV absorbance and Bradford assay." Biophysics Reports 7 (2022): 1–8. http://dx.doi.org/10.52601/bpr.2022.210028.

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Jiang, Chen, Luo Hao, Tao Mei, Liu Zhongchuan, and Wang Ganggang. "Quantitation of nucleoprotein complexes by UV absorbance and Bradford assay." Biophysics Reports 7, no. 6 (2021): 429–36. http://dx.doi.org/10.52601/bpr.2021.210028.

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Zhang, Chenji, Gong Cheng, Perry Edwards, Ming-Da Zhou, Siyang Zheng, and Zhiwen Liu. "G-Fresnel smartphone spectrometer." Lab on a Chip 16, no. 2 (2016): 246–50. http://dx.doi.org/10.1039/c5lc01226k.

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We report a smartphone spectrometer with nanometer resolution working in the visible range. A G-Fresnel device with the dual functionality of focusing and dispersion is used to enable miniaturization. Proof of principle application to Bradford assay of protein concentration is also demonstrated.

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LEA, MICHAEL A., ALEYKUTTY LUKE, CHARLES MARTINSON, and OMAIDA VELAZQUEZ. "Effect of Cyanate on Assay of Proteins by the Bradford Procedure." Annals of the New York Academy of Sciences 463, no. 1 Second Colloq (May 1986): 109–11. http://dx.doi.org/10.1111/j.1749-6632.1986.tb21515.x.

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Compton, Steve J., and Clive G. Jones. "Mechanism of dye response and interference in the Bradford protein assay." Analytical Biochemistry 151, no. 2 (December 1985): 369–74. http://dx.doi.org/10.1016/0003-2697(85)90190-3.

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Crespo, André L. B., Terence A. Spencer, Emily Nekl, Marianne Pusztai-Carey, William J. Moar, and Blair D. Siegfried. "Comparison and Validation of Methods To Quantify Cry1Ab Toxin from Bacillus thuringiensis for Standardization of Insect Bioassays." Applied and Environmental Microbiology 74, no. 1 (November 2, 2007): 130–35. http://dx.doi.org/10.1128/aem.01855-07.

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ABSTRACT Standardization of toxin preparations derived from Bacillus thuringiensis (Berliner) used in laboratory bioassays is critical for accurately assessing possible changes in the susceptibility of field populations of target pests. Different methods were evaluated to quantify Cry1Ab, the toxin expressed by 80% of the commercially available transgenic maize that targets the European corn borer, Ostrinia nubilalis (Hübner). We compared three methods of quantification on three different toxin preparations from independent sources: enzyme-linked immunosorbent assay (ELISA), sodium dodecyl sulfate-polyacrylamide gel electrophoresis and densitometry (SDS-PAGE/densitometry), and the Bradford assay for total protein. The results were compared to those obtained by immunoblot analysis and with the results of toxin bioassays against susceptible laboratory colonies of O. nubilalis. The Bradford method resulted in statistically higher estimates than either ELISA or SDS-PAGE/densitometry but also provided the lowest coefficients of variation (CVs) for estimates of the Cry1Ab concentration (from 2.4 to 5.4%). The CV of estimates obtained by ELISA ranged from 12.8 to 26.5%, whereas the CV of estimates obtained by SDS-PAGE/densitometry ranged from 0.2 to 15.4%. We standardized toxin concentration by using SDS-PAGE/densitometry, which is the only method specific for the 65-kDa Cry1Ab protein and is not confounded by impurities detected by ELISA and Bradford assay for total protein. Bioassays with standardized Cry1Ab preparations based on SDS-PAGE/densitometry showed no significant differences in LC50 values, although there were significant differences in growth inhibition for two of the three Cry1Ab preparations. However, the variation in larval weight caused by toxin source was only 4% of the total variation, and we conclude that standardization of Cry1Ab production and quantification by SDS-PAGE/densitometry may improve data consistency in monitoring efforts to identify changes in insect susceptibility to Cry1Ab.

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Chalermrujinanant, Chonvara, Panwadee Pluangnooch, and Kitipong Soontrapa. "Evaluation of 3 Common Methods for Effective Housefly Allergen Extraction." Ramathibodi Medical Journal 44, no. 1 (March 26, 2021): 40–45. http://dx.doi.org/10.33165/rmj.2021.44.1.245935.

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Background: Allergen extracts have been applied to treat allergic diseases. Accordingly, a housefly (Musca domestica) extract is commonly used to treat patients severely allergic to housefly. Objective: To evaluate 3 common methods, including grinding, sonication, and homogenization, for effective preparation of housefly allergen extracts. Methods: Housefly allergens were extracted from Musca domestica using 3 different methods, including grinding, sonication, and homogenization. Protein concentrations and profiles in the extracts were determined by Bradford assay and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), respectively. Results: The protein concentrations of the extracts prepared by grinding (mean [SD], 911.3 [159.7] µg/µL) and sonication (mean [SD], 905.7 [188.6] µg/µL) as measured by Bradford assay were significantly higher than those prepared by homogenization (mean [SD], 674.5 [60.0] µg/µL). Moreover, SDS-PAGE showed more protein bands in the extracts prepared using grinding and sonication compared to those prepared using homogenization. Conclusions: In comparison to homogenization, both grinding and sonication methods are superior ways to prepare housefly allergen extracts as evidenced by the higher quantities and composition of proteins.

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Babaei-Afrapoli, Zoha, Reza Faridi-Majidi, Babak Negahdari, Keyvan Dabir, and Gholamreza Tavoosidana. "Evaluating gold nanoparticles parameters in competitive Immunochromatographich Assay via Dot Blot and Bradford Assay as new approaches." Microchemical Journal 170 (November 2021): 106525. http://dx.doi.org/10.1016/j.microc.2021.106525.

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Zanini, Leonardo, Annamaria Zaltron, Enrico Turato, Riccardo Zamboni, and Cinzia Sada. "Opto-Microfluidic Integration of the Bradford Protein Assay in Lithium Niobate Lab-on-a-Chip." Sensors 22, no. 3 (February 2, 2022): 1144. http://dx.doi.org/10.3390/s22031144.

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This paper deals with the quantification of proteins by implementing the Bradford protein assay method in a portable opto-microfluidic platform for protein concentrations lower than 1.4 mg/mL. Absorbance is measured by way of optical waveguides integrated to a cross-junction microfluidic circuit on a single lithium niobate substrate. A new protocol is proposed to perform the protein quantification based on the high correlation of the light absorbance at 595 nm, as commonly used in the Bradford method, with the one achieved at 633 nm with a cheap commercially available diode laser. This protocol demonstrates the possibility to quantify proteins by using nL volumes, 1000 times less than the standard technique such as paper-analytical devices. Moreover, it shows a limit of quantification of at least 0.12 mg/mL, which is four times lower than the last literature, as well as a better accuracy (98%). The protein quantification is obtained either by using one single microfluidic droplet as well by performing statistical analysis over ensembles of several thousands of droplets in less than 1 min. The proposed methodology presents the further advantage that the protein solutions can be reused for other investigations and the same pertains to the opto-microfluidic platform.

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CARROLL, KENNETH, and RICHARD O'KENNEDY. "Interference effects from Nonidet P-40 and urea in the Bradford protein assay." Biochemical Society Transactions 16, no. 3 (June 1, 1988): 382–83. http://dx.doi.org/10.1042/bst0160382a.

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Friedenauer, Susanne, and Hans H. Berlet. "Sensitivity and variability of the Bradford protein assay in the presence of detergents." Analytical Biochemistry 178, no. 2 (May 1989): 263–68. http://dx.doi.org/10.1016/0003-2697(89)90636-2.

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Wenrich, Broc R., and Toni A. Trumbo. "Interaction of nucleic acids with Coomassie Blue G-250 in the Bradford assay." Analytical Biochemistry 428, no. 2 (September 2012): 93–95. http://dx.doi.org/10.1016/j.ab.2012.06.014.

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Ku, Hyung-Keun, Hyuk-Min Lim, Kyong-Hwa Oh, Hyo-Jin Yang, Ji-Seon Jeong, and Sook-Kyung Kim. "Interpretation of protein quantitation using the Bradford assay: Comparison with two calculation models." Analytical Biochemistry 434, no. 1 (March 2013): 178–80. http://dx.doi.org/10.1016/j.ab.2012.10.045.

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Zor, Tsaffrir, and Zvi Selinger. "Linearization of the Bradford Protein Assay Increases Its Sensitivity: Theoretical and Experimental Studies." Analytical Biochemistry 236, no. 2 (May 1996): 302–8. http://dx.doi.org/10.1006/abio.1996.0171.

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Gazzola, Diana, Simone Vincenzi, Gabriella Pasini, Giovanna Lomolino, and Andrea Curioni. "Advantages of the KDS/BCA Assay over the Bradford Assay for Protein Quantification in White Wine and Grape Juice." American Journal of Enology and Viticulture 66, no. 2 (December 12, 2014): 227–33. http://dx.doi.org/10.5344/ajev.2014.14076.

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Balciunaite, Gabriele, Jovita Juodsnukyte, Arunas Savickas, Ona Ragazinskiene, Luka Siatkute, Gitana Zvirblyte, Edita Mistiniene, and Nijole Savickiene. "Fractionation and evaluation of proteins in roots of Echinacea purpurea (L.) Moench." Acta Pharmaceutica 65, no. 4 (December 1, 2015): 473–79. http://dx.doi.org/10.1515/acph-2015-0036.

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Abstract Echinacea purpurea (L.) Moench, a member of the Asteraceae family, is a plant rich in flavonoids, essential oils, phenolic compounds, saponins, polysaccharides and glycoproteins. The aim of the study was to evaluate the protein content in dried roots of Echinacea purpurea (L.) Moench after homogenization of roots with liquid nitrogen, extraction in 0.01 mol L-1 phosphate-buffered saline (PBS) and purification followed by fractionation of proteins using gel filtration chromatography. Total concentration of proteins was measured using the Bradford method, and evaluation of the molecular mass of proteins was accomplished by applying the SDS-PAGE gel electrophoresis. The Bradford assay revealed that the highest concentration of proteins in fractions collected after gel filtration chomatography was 4.66–6.07 mg mL-1. Glycoproteins, alkamides and polysaccharides in roots of Echinacea purpurea (L.) Moench are chemical compounds that are responsible for their immunomodulatory properties. However, information about the difference of protein contents in fresh and dried roots of E. purpurea is insufficient.

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Betti, Michele, Caterina Ciacci, Sigal Abramovich, and Fabrizio Frontalini. "Protein Extractions from Amphistegina lessonii: Protocol Development and Optimization." Life 11, no. 5 (May 5, 2021): 418. http://dx.doi.org/10.3390/life11050418.

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Proteins are essential to life, and the evaluation of their content, identification, and modification represents a fundamental assay in biochemistry research. Different analytical techniques and protocols have been specifically designed but have rarely been compared. Here, we test and compare a variety of methodologies and treatments for the quantification of proteins in Amphistegina lessonii, a larger symbiont-bearing benthic foraminiferal species. These analyses specifically include (a) lysis buffer (homemade vs. RIPA), (b) protein assays (Lowry, BCA, and Bradford), (c) ultrasonic bath treatment, and (d) protein staining (silver staining vs. Coomassie blue). On the basis of the comparative outcome, we suggest using the homemade lysis buffer, Lowry or BCA assays, ultrasonic bath treatment, and silver stain to maximize the extraction and characterization of protein for A. lessonii. This protocol might be suitable and extended to other benthic foraminiferal species, including the smaller ones.

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Silva, A. L. S., A. S. Nunes, and J. L. Gesztesi Natura. "Protein loss quantification of abraded virgin and abraded bleached hair according to Bradford assay." International Journal of Cosmetic Science 27, no. 2 (April 2005): 139–40. http://dx.doi.org/10.1111/j.1467-2494.2005.00257_14.x.

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Mehata, Abhishesh Kumar, and Deepa Dehari. "Bradford assay as a high-throughput bioanalytical screening method for conforming pathophysiological state of the animal." Journal of Drug Delivery and Therapeutics 10, no. 1-s (February 15, 2020): 105–10. http://dx.doi.org/10.22270/jddt.v10i1-s.3921.

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Proteins are the essential components of the tissues that play a key role in the body. Its expression in the cell or tissue under a specified set of conditions and at a particular time regulates the different body conditions either as a normal body function or as a disease state. Protein is an important building block of muscles, skin, cartilage, bones and blood. Bradford assay is a reliable advanced and cost-effective protein estimation test for determining the exact concentration of protein in different tissues of the animal. In this study, we have taken a rat suffering from protein deficiency disorder and total protein concentration in the heart, brain, liver, blood and kidney was determined. It was found that the total protein concentration in different tissues of rat i.e., heart, brain, liver, plasma and kidney was found to be 8.39 ± 0.75, 10.46 ± 0.76, 6.74 ± 0.39, 8.12 ± 0.32 mg/g of tissue and 61.27 ± 0.95 mg/mL of plasma respectively (mean ± SEM). As compared to earlier published reports the total protein concentration in different tissues like hear, brain, liver and kidney found much lower to standard value as reported by Beyer, the reason behind obtaining this kind of results may be due to the presence of insufficient amount of the protein content in different tissue of animal as suffering from protein degeneration disorder. The rat was unable to digest and store the protein or catabolism was much faster than anabolism. Keywords: Anabolism, Bradford assay, Catabolism, Protein estimation.

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Cui, Weitong, Huaru Xue, Hongda Cheng, Haibin Zhang, Jinghua Jin, and Qinglu Wang. "Increasing the amount of phosphoric acid enhances the suitability of Bradford assay for proteomic research." ELECTROPHORESIS 40, no. 7 (January 4, 2019): 1107–12. http://dx.doi.org/10.1002/elps.201800430.

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Sherovski, Pece, Goran Stojković, and Natasha Ristovska. "Development, validation and application of first derivative spectroscopy ratio method for estimation of Bradford assay." Analytical Biochemistry 558 (October 2018): 35–40. http://dx.doi.org/10.1016/j.ab.2018.07.027.

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Fanger, Bradford O. "Adaptation of the Bradford protein assay to membrane-bound proteins by solubilizing in glucopyranoside detergents." Analytical Biochemistry 162, no. 1 (April 1987): 11–17. http://dx.doi.org/10.1016/0003-2697(87)90004-2.

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Sunarwidhi, A. L., A. Rosyantari, E. S. Prasedya, N. Ardiana, B. T. K. Ilhami, A. S. Abidin, Y. Ambana, et al. "The correlation between total protein content and antioxidant activity of collagen isolated from a marine sponge Stylissa flabelliformis collected from North Lombok Indonesia coast." IOP Conference Series: Earth and Environmental Science 913, no. 1 (November 1, 2021): 012103. http://dx.doi.org/10.1088/1755-1315/913/1/012103.

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Abstract Abstract.Collagen is a fibrous protein that has recently gained high attention from the pharmaceutical industry due to its benefits on the skin. Collagen can be isolated from various resources including marine sponges. Marine sponges are found in a large amount in Indonesia and has not been widely explored for its pharmacology benefits. Here we isolate collagen from a marine sponge Stylissa flabelliformis found in North Lombok Indonesia coast. The isolation of collagen was performed followed by total protein content analysis using modified Bradford protein assay and antioxidant activity measurement using 2,2-diphenyl-1-picrylhydrazyl(DPPH) assay. The total yield of the collagen isolate obtained was 3.5% and it had a total of 0.755mg/ml protein. DPPH assay has shown that the collagen isolate had antioxidant activity with an IC50 of 61.5±2.132 ppm. Based on Spearman correlation assay, the antioxidant activity was found to be correlated with the protein content of the isolate (r value=0.8). These results show the potency of using the collagen isolated from marine sponge Stylissa flabelliformis for further antioxidant benefits.

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Khramtsov, Pavel, Tatyana Kalashnikova, Maria Bochkova, Maria Kropaneva, Valeria Timganova, Svetlana Zamorina, and Mikhail Rayev. "Measuring the concentration of protein nanoparticles synthesized by desolvation method: Comparison of Bradford assay, BCA assay, hydrolysis/UV spectroscopy and gravimetric analysis." International Journal of Pharmaceutics 599 (April 2021): 120422. http://dx.doi.org/10.1016/j.ijpharm.2021.120422.

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Baharun, A., I. Arifiantini, N. W. K. Karja, and S. Said. "Seminal plasma protein profile based on molecular weight and their correlation with semen quality of Simmental bull." Journal of the Indonesian Tropical Animal Agriculture 46, no. 1 (November 11, 2020): 20–28. http://dx.doi.org/10.14710/jitaa.46.1.20-28.

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Artificial Insemination Center (AIC) produces frozen semen that was taken from superior bull. The selection of superior bull was based on breeding soundness evaluation. This study is aimed to evaluating the correlation between the molecular weight (MW) of seminal plasma protein and semen quality of Simmental bulls. Semen ejaculates from nine Simmental Bulls, that belong to AIC of Central Java, at Ungaran, were collected by using an artificial vagina. The sub population of sperm in ejaculates was evaluated through macroscopically and microscopically, in which the semen then centrifugated 6500 rpm for 30 minutes. The supernatant was collected and inserted into mini straw and stored in liquid nitrogen container. The concentration of seminal plasma protein was determined by the Bradford method. The Bradford protocol of analysis was suitable with User Guide Coomasize (Bradford) Protein Assay Kit. Thermo Skanlt RE for Multiskan Go Software, 3.2 version was applied for analyzing of the data, and protein characterization used was 1D-SDS-PAGE. The Coomassie Brilliant Blue was used for coloring the gels, and the proteins MW was determined by MW markers. The result demonstrated that there was no significant correlation between protein concentration and semen quality (P>0.05). Protein expressions based on MW were 62-48 kD, 100-71 kD found in this study. The analysis of correlation showed that the proteins with 100-71 kD MW correlated with sperm motility, normal sperm morphology, and sperm concentration. Semen quality in all parameters was significant (P˂0.05 and P>0.01) with 62-48 kD protein MW. The result concluded that seminal plasma protein had a correlation with semen quality and can be used as additional indicator for bull’s candidate selection.

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Taher, Nehad A. "Antimicrobial Effect of Bacteriocin produced Pediococcus pentosaceus on some clinical isolates." Al-Mustansiriyah Journal of Science 27, no. 5 (July 6, 2017): 26. http://dx.doi.org/10.23851/mjs.v27i5.163.

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About 10 isolates of Pediococcus sp were isolated from different cheese made in Iraq, These isolates were identified morphologically and biochemically and Api20 kit, thus there was only 6 isolate were identified as Pediococcus pentosaceus (60%).In this study, we investigate, the effect of crude Bacteriocin from Pediococcus pentosaceus on 30 clinical isolates (5 E.coli, 5 Klepsiella pneumoniae, 5 Staphylococcus aureus, 5 Pseudomonas aeroginosa, 5 Bacillus subtilis, 5 Candida albicans). The protein concentration of this Bacteriocin was measured 67mg\ml by Bradford method and used as (1:2) by vol during the measuring the antimicrobial activity against the above clinical isolates by two methods wells and agar plug assay. The results showed that the inhibitory activity of this Bacteriocin was higher by wells method than agar pluq assay against Gram–positive bacteria or Gram-negative bacteria and yeast under this study.

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Sissolak, Bernhard, Christian Zabik, Natasa Saric, Wolfgang Sommeregger, Karola Vorauer‐Uhl, and Gerald Striedner. "Application of the Bradford Assay for Cell Lysis Quantification: Residual Protein Content in Cell Culture Supernatants." Biotechnology Journal 14, no. 7 (May 17, 2019): 1800714. http://dx.doi.org/10.1002/biot.201800714.

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Cheng, Yongfeng, Haiming Wei, Rui Sun, Zhigang Tian, and Xiaodong Zheng. "Rapid method for protein quantitation by Bradford assay after elimination of the interference of polysorbate 80." Analytical Biochemistry 494 (February 2016): 37–39. http://dx.doi.org/10.1016/j.ab.2015.10.013.

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Bercansil, Mia Clare Marie L., and Miko Lorenzo J. Belgado. "Anti-coagulant Activity of Isolated and Partially Characterized Proteoglycans and Glycosaminoglycans from African Night Crawler (Eudrilus eugeniae Kinberg)." KIMIKA 26, no. 2 (November 14, 2015): 31–38. http://dx.doi.org/10.26534/kimika.v26i2.31-38.

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Proteoglycans and glycosaminoglycans were isolated from African night crawler (Eudrilus eugeniae Kinberg) and partially characterized proteoglycans (3.04 % of lyophilized worm) were liberated from the defatted and depurinated worm samples by dissociative method using 4M urea in acetate buffer. Glycosaminoglycans (12.47% of proteoglycan extract) were extracted using enzymatic hydrolysis of the proteoglycan extract with papain. Gel filtration chromatography using Sepharose CL-4B was used to purify and estimate the molecular weights of the proteoglycan and glycosaminoglycan fractions. Three proteoglycan fractions PGF1, PGF2 and PGF3 with estimated molecular weigths 860 kDa, 181 kDa and 3 kDa, respectively were identified as monitored by the Bradford and modified carbazole assay. Two glycosaminoglycan fractions - GF1 (MW = 860 kDa) and GF2 (MW=140 kDa) were identified using the modified carbazole assay. Infrared spectroscopy of the GF1 and GF2 showed the possible identities of the fractions. GF1 may be a hyaluronic acid and GF2 is possibly chondroitin. Anti-coagulant assay for the extracts and fractions revealed that the glycosaminoglycan isolate has anti-coagulant activity but not the GF1 and GF2 fractions individually.

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Wu, Kuo-Hui, Wen-Chien Huang, Shu-Chen Chang, Ching-Hua Kao, and Rong-Hwa Shyu. "Preparation of competitive immunochromatographic assay for detection of residual fipronil in urine and food samples." Materials Express 11, no. 1 (January 1, 2021): 63–72. http://dx.doi.org/10.1166/mex.2021.1889.

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A colloidal silver nanoparticle (AgNP)-based lateral flow immunoassay (LFIA) was developed using an antifipronil polyclonal antibody (fAb), and its employment for the rapid detection of residual fipronil in spiked egg, honey, tea and human urine samples was studied. The fAb was successfully immobilized on the AgNP surface by ionic interactions and characterized using the Bradford method, UV-Vis, SEM, TEM and XPS analyses. The visible detection limit and optical detection limit of the fipronil test strip were 40 and 2.0 ppb, respectively, in fipronil standard solution. This assay showed no cross-reaction with pyraclofos or ethiprole. Finally, the fipronil test strip was effectively applied for the detection of fipronil spiked into egg, honey, tea and urine samples, with optical detection limits of 4.6, 10, 4.6 and 3.0 ppb, respectively. The results demonstrated that this assay is suitable for the quantitative detection of fipronil at trace levels in agricultural, food and urine samples.

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Lee, Jong-Won, Kyoung-Bong Ha, Youn-Kyu Kim, Joo-Hee Lee, In-Ho Choi, and Seul-Hyun Park. "Media Exchange Performance Test Using the Bradford Assay in an Automated Bioreactor Engineering Model for Space Experiments." SLAS TECHNOLOGY: Translating Life Sciences Innovation 24, no. 2 (August 10, 2018): 222–32. http://dx.doi.org/10.1177/2472630318794130.

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Life science research has been actively carried out in space for a long time using bioreactor equipment, in anticipation of manned space exploration and space tourism. Such studies have reported that the microgravity environment has a negative effect on the human body, including the musculoskeletal system, nervous system, and endocrine system. Bone loss and muscular atrophy are issues that need to be resolved before long-term exposure of the human body to a space environment. To address this problem, Y. K. Kim et al. designed a system in 2015 and performed an evaluation of an automated bioreactor development model (DM) for space experiments. In this study, we developed an automated bioreactor engineering model (EM) based on the previous literature, and conducted media exchange performance testing using the Bradford assay. We used a novel method that allowed quantitative assessment of the media exchange rate versus the conventional assessment method using visual observation with a camera. By measuring the media exchange rate of the automated bioreactor EM, we attempted to verify applicability for the system for space experiments. We expect that the experimental method proposed in this study is useful for logical determination of liquid exchange or circulation in different closed systems.

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Aminian, Mahdi, Fariba Nabatchian, Asad Vaisi-Raygani, and Mojgan Torabi. "Mechanism of Coomassie Brilliant Blue G-250 binding to cetyltrimethylammonium bromide: An interference with the Bradford assay." Analytical Biochemistry 434, no. 2 (March 2013): 287–91. http://dx.doi.org/10.1016/j.ab.2012.11.014.

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Boonsriwong, Worachote, Suticha Chunta, Nonthawat Thepsimanon, Sanita Singsanan, and Peter A. Lieberzeit. "Thin Film Plastic Antibody-Based Microplate Assay for Human Serum Albumin Determination." Polymers 13, no. 11 (May 27, 2021): 1763. http://dx.doi.org/10.3390/polym13111763.

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Herein we demonstrate molecularly imprinted polymers (MIP) as plastic antibodies for a microplate-based assay. As the most abundant plasma protein, human serum albumin (HSA) was selected as the target analyte model. Thin film MIP was synthesized by the surface molecular imprinting approach using HSA as the template. The optimized polymer consisted of acrylic acid (AA) and N-vinylpyrrolidone (VP) in a 2:3 (w/w) ratio, crosslinked with N,N′-(1,2-dihydroxyethylene) bisacrylamide (DHEBA) and then coated on the microplate well. The binding of MIP toward the bound HSA was achieved via the Bradford reaction. The assay revealed a dynamic detection range toward HSA standards in the clinically relevant 1–10 g/dL range, with a 0.01 g/dL detection limit. HSA-MIP showed minimal interference from other serum protein components: γ-globulin had 11% of the HSA response, α-globulin of high-density lipoprotein had 9%, and β-globulin of low-density lipoprotein had 7%. The analytical accuracy of the assay was 89–106% at the 95% confidence interval, with precision at 4–9%. The MIP-coated microplate was stored for 2 months at room temperature without losing its binding ability. The results suggest that the thin film plastic antibody system can be successfully applied to analytical/pseudoimmunological HSA determinations in clinical applications.

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Rogers, Suzanne M. D., and Kalyani Dias. "EFFECT OF SALT SHOCK ON PHOTOMIXOTROPHIC SUSPENSION CULTURES OF SOYBEAN." HortScience 25, no. 9 (September 1990): 1149e—1149. http://dx.doi.org/10.21273/hortsci.25.9.1149e.

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When plants are subjected to stress conditions, they are believed to be developing defensive mechanisms. Those mechanisms could be studied by analysing and comparing the proteins from stressed and nonstressed plant materials. Photomixotrophically grown soybean suspension cultures were shocked with 150 mM, 200 mM, and 250 mM salt concentrations for 1 hr. and 3 hrs. The cells were then given 2, or 4 hr. recovery period. After treatment, proteins were quantified, using Bradford Assay, and then separated on SDS PAGE gels. In Coomasie stained gells, there were different banding patterns in shock treated samples, compared to the control. But there were no differences identified between different shocking times or recovery period treatments. The results from Silver staining and growth studies will be presented.

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Shukla, Shruti. "A Bradford multiplexing method for protein estimation in fermented foods: Soy sauces." Bangladesh Journal of Pharmacology 11, no. 1 (December 16, 2015): 24. http://dx.doi.org/10.3329/bjp.v11i1.25796.

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Proteins for foods, in addition to providing nutrition, should also possess specific functional properties that facilitate processing and serve as the basis of product performance. Soy protein is a major component of the diet of food and is increasingly important in the human diet. Hence, here in the present article, we are focusing a rapid and easy method for quantitative determination of total protein content with multiplex samples in any food products such as soy sauce or other traditional fermented foods. We described a bioassay procedure (Bradford method) for the evaluation of total protein content in foods. This method involves measurement of the protein efficiency ratio under standardized conditions. The experiment will provide researchers a scientific way to determine pretentious quality of variety of foods and/or health supplements. VIDEO CLIPS<a href="https://www.youtube.com/v/xVzg0rq4VxE">Requirement and sample preparation method:</a> 3 min 26 sec<a href="https://www.youtube.com/v/6plwYgGGFuE">Assay procedure:</a> 6 min 4 sec<a href="https://www.youtube.com/v/bV2tGWLh4ug">Measurement of absorbance using an ELISA microtiter plate reader:</a>5 min 1 sec

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Marshall, Thomas, and Katherine M. Williams. "Phenol addition to the Bradford dye binding assay improves sensitivity and gives a characteristic response with different proteins." Journal of Biochemical and Biophysical Methods 13, no. 3 (October 1986): 145–50. http://dx.doi.org/10.1016/0165-022x(86)90087-4.

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Montegiove, Nicolò, Roberto Maria Pellegrino, Carla Emiliani, Alessia Pellegrino, and Leonardo Leonardi. "An Alternative Approach to Evaluate the Quality of Protein-Based Raw Materials for Dry Pet Food." Animals 11, no. 2 (February 9, 2021): 458. http://dx.doi.org/10.3390/ani11020458.

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The majority of dry pet food currently on the market is produced using fresh meats (FMs) and especially meat meals (MMs) as the main protein source. The transport and storage conditions of the raw materials, together with thermal and mechanical treatments in the case of MMs, may result in undesirable alterations of food products and their protein content. This study was conducted to analyze the protein component of three different kinds of raw materials used for dry pet food production, i.e., chicken, pork, and salmon. The quantitative analysis of the protein component was determined using the traditional Kjeldahl method and near-infrared (NIR) spectroscopy, and an alternative method, i.e., the Bradford assay, while the qualitative analysis was performed through SDS-PAGE, followed by Coomassie Blue staining. The amino acid (AA) profile was also evaluated by quadrupole time-of-flight liquid chromatography/mass spectrometry (Q-TOF LC/MS). In addition, the digestibility was tested through in vitro gastric and small intestine digestion simulation. Statistical analysis was performed by the Student’s t-test, and data are reported as mean ± SEM, n = 10 (p < 0.05). The results showed that the MMs are lower in quality compared to FMs, both in terms of protein bioavailability and digestibility, having a lower soluble protein (SP) content (chicken MM = 8.6 g SP/100 g dry sample; pork MM = 6.2 g SP/100 g dry sample; salmon MM = 7.9 g SP/100 g dry sample) compared to FMs (chicken FM = 14.6 g SP/100 g dry sample; pork FM = 15.1 g SP/100 g dry sample; salmon FM = 13.7 g SP/100 g dry sample). FMs appear, therefore, to be higher-quality ingredients for pet food production. Moreover, the Bradford assay proved to be a quick and simple method to better estimate protein bioavailability in the raw materials used for dry pet food production, thanks to its correlation with the in vitro digestibility.

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Gonçalves, Luiz Guilherme Cruz, Rodrigo Leal de Queiroz Thomaz de Aquino, and Enrico Fuini Puggina. "Long distance run induced hydration and kidney function changes in marathoners." Motriz: Revista de Educação Física 21, no. 3 (September 2015): 299–304. http://dx.doi.org/10.1590/s1980-65742015000300011.

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AbstractThe aim of the study was to verify the hydration status and the kidney function in marathoners during the training season and after a marathon race. Nine male runners were investigated during 12 weeks of training. Urine was collected in four moments; in the beginning (C1) and during (C2) the training program, before (C3) and after (C4) the competition. Urine pH was measured using reagent tapes, urine density with a refractometer, protein excretion by Bradford assay and erythrocytes and leucocytes by microscopy. Changes were observed when C-4 was compared to the other collection times for all variables investigated. It is possible to conclude that physical exertion induced important changes in the hydration status and glomerular membrane selectivity to macromolecules, modifying the kidney function of the marathoners in C4.

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Wang, Ting, and Li Guo. "The Optimization of Synthesis Condition of ZnSe Nanocrystals." Advanced Materials Research 534 (June 2012): 61–64. http://dx.doi.org/10.4028/www.scientific.net/amr.534.61.

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In biomineralization, self-organization of organic based templates provides scaffolding for the assembly of QDs materials. The host-guest relationship between these protein cages and the encapsulated material is based primarily on a complementary electrostatic interaction. Zinc selenide (ZnSe) were synthesized in the cavity of the apoferritin from horse spleen (HsAFr) and the reaction condition was optimized by adding tween 20 to avoid ferritin agglomeration. The obtained nanodots were characterized by TEM, and absorption measurements. In addition, the protein concentration of ZnSe-ferritin was precisely measured by the Bradford protein assay method. From the results, it was concluded that the ZnSe nanocrystals were successfully synthesized in the core of ferritin and it can be applied as a potential functional material such as transistors, biosensor materials or medical imaging.

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Journal articles on the topic 'Bradford assay'

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