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A multipurpose solid-phase method for protein determination with Coomassie brilliant blue G-250.

作者信息

Said-Fernández S, González-Garza M T, Mata-Cárdenas B D, Navarro-Marmolejo L

机构信息

Unidad de Investigación Biomédica del Noreste, Instituto Mexicano del Seguro Social, Nuevo León, México.

出版信息

Anal Biochem. 1990 Nov 15;191(1):119-26. doi: 10.1016/0003-2697(90)90397-r.

DOI:10.1016/0003-2697(90)90397-r
PMID:1706563
Abstract

The multipurpose method for protein determination (MMPD) is based in the Coomassie brilliant blue G-250 binding to immobilized and washed proteins in paper filter disks, and the A600 measurement of the eluted protein-dye complexes. The analysis requires 5-microliters samples, put in 7-mm paper filter disks, which can be stored for up to 2 weeks, without sensible changes in their protein content. The A600 is a logarithmic function of the log of bovine serum albumin quantity, between 2.5 and 250 micrograms with two linear segments used as standard curves: one between 2.5 to 20 micrograms and the other between 20 and 80 micrograms. Results with the MMPD were quantitatively comparable with those obtained with the method of Lowry et al., and those reported by other workers, assaying the following material: (i) bovine serum albumin, in doubly distilled water or in presence of several substances that interfere with the current methods; and (ii) total homogenates and their respective trichloroacetic acid-insoluble extracts, which were obtained from several phenol-rich vegetal specimens and complex animal products. The MMPD is proposed as an alternative for protein determination for its versatility and reliability, in both vegetal or animal products, especially when the analysis with traditional methods is made difficult by the presence of natural or added interfering substances and the sample volume is too small to discard them, or when the material must be stored for relatively long periods of time, prior to its processing.

摘要

相似文献

1
A multipurpose solid-phase method for protein determination with Coomassie brilliant blue G-250.
Anal Biochem. 1990 Nov 15;191(1):119-26. doi: 10.1016/0003-2697(90)90397-r.
2
Protein assay by Coomassie brilliant blue G-250-binding method is unsuitable for plant tissues rich in phenols and phenolases.采用考马斯亮蓝G - 250结合法进行蛋白质测定不适用于富含酚类和酚酶的植物组织。
Anal Biochem. 1987 Jun;163(2):376-84. doi: 10.1016/0003-2697(87)90238-7.
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Criticism of the use of Coomassie Brilliant Blue G-250 for the quantitative determination of proteins.对使用考马斯亮蓝G - 250进行蛋白质定量测定的批评。
J Clin Chem Clin Biochem. 1981 May;19(5):301-4. doi: 10.1515/cclm.1981.19.5.301.
4
Quantitation of electrophoretic eluted proteins.电泳洗脱蛋白质的定量分析。
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Refinement of the Coomassie brilliant blue G assay for quantitative protein determination.考马斯亮蓝G法用于蛋白质定量测定的优化。
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Quantitation of proteins by elution of Coomassie brilliant blue R from stained bands after sodium dodecyl sulfate-polyacrylamide gel electrophoresis.十二烷基硫酸钠-聚丙烯酰胺凝胶电泳后,通过从染色条带中洗脱考马斯亮蓝R来定量蛋白质。
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Coomassie-Brilliant Blue staining of polyacrylamide gels.聚丙烯酰胺凝胶的考马斯亮蓝染色。
Methods Mol Biol. 2012;869:465-9. doi: 10.1007/978-1-61779-821-4_40.
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[Method of determination of proteins with Coomassie brilliant blue G 250. I. General characteristics and comparative analysis with the biuret method and Lowry's method].[考马斯亮蓝G 250法测定蛋白质。I. 一般特性及与双缩脲法和洛瑞法的比较分析]
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