Protein analysis with bicinchoninic acid
Some of the variables and the interferences which affect the reaction kinetics of proteins with bicinchoninic acid (BCA) (4,4'-dicarboxy-2,2'-biquinoline) have been studied. Interferences attributed to glucose, ascorbic acid, and uric acid in this reaction were significantly reduced by per...
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| Veröffentlicht in: | Annals of clinical and laboratory science 1988-05, Vol.18 (3), p.235-239 |
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| container_title | Annals of clinical and laboratory science |
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| creator | SHIHABI, Z. K DYER, R. D |
| description | Some of the variables and the interferences which affect the reaction kinetics of proteins with bicinchoninic acid (BCA) (4,4'-dicarboxy-2,2'-biquinoline) have been studied. Interferences attributed to glucose, ascorbic acid, and uric acid in this reaction were significantly reduced by performing a two-point assay and by including borate ions in the buffer. The method was shown to be suitable for automation and can be applied for the analysis of protein in physiological fluids, such as cerebrospinal fluid and cells grown in tissue cultures. The method compared well with other established methods for protein assays, such as the Coomassie blue and the turbidimetric method, and it is more sensitive to globulins than albumins. |
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K ; DYER, R. D</creator><creatorcontrib>SHIHABI, Z. K ; DYER, R. D</creatorcontrib><description>Some of the variables and the interferences which affect the reaction kinetics of proteins with bicinchoninic acid (BCA) (4,4'-dicarboxy-2,2'-biquinoline) have been studied. Interferences attributed to glucose, ascorbic acid, and uric acid in this reaction were significantly reduced by performing a two-point assay and by including borate ions in the buffer. The method was shown to be suitable for automation and can be applied for the analysis of protein in physiological fluids, such as cerebrospinal fluid and cells grown in tissue cultures. The method compared well with other established methods for protein assays, such as the Coomassie blue and the turbidimetric method, and it is more sensitive to globulins than albumins.</description><identifier>ISSN: 0091-7370</identifier><identifier>EISSN: 1550-8080</identifier><identifier>PMID: 3389719</identifier><identifier>CODEN: ACLSCP</identifier><language>eng</language><publisher>Philadelphia, PA: Institute for Clinical Science</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Drug Contamination ; Fundamental and applied biological sciences. 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D</creatorcontrib><title>Protein analysis with bicinchoninic acid</title><title>Annals of clinical and laboratory science</title><addtitle>Ann Clin Lab Sci</addtitle><description>Some of the variables and the interferences which affect the reaction kinetics of proteins with bicinchoninic acid (BCA) (4,4'-dicarboxy-2,2'-biquinoline) have been studied. Interferences attributed to glucose, ascorbic acid, and uric acid in this reaction were significantly reduced by performing a two-point assay and by including borate ions in the buffer. The method was shown to be suitable for automation and can be applied for the analysis of protein in physiological fluids, such as cerebrospinal fluid and cells grown in tissue cultures. The method compared well with other established methods for protein assays, such as the Coomassie blue and the turbidimetric method, and it is more sensitive to globulins than albumins.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Drug Contamination</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>General aspects, investigation methods</topic><topic>Hydrogen-Ion Concentration</topic><topic>Proteins</topic><topic>Proteins - analysis</topic><topic>Quinolines</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SHIHABI, Z. K</creatorcontrib><creatorcontrib>DYER, R. D</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Annals of clinical and laboratory science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SHIHABI, Z. K</au><au>DYER, R. 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The method compared well with other established methods for protein assays, such as the Coomassie blue and the turbidimetric method, and it is more sensitive to globulins than albumins.</abstract><cop>Philadelphia, PA</cop><pub>Institute for Clinical Science</pub><pmid>3389719</pmid><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0091-7370 |
| ispartof | Annals of clinical and laboratory science, 1988-05, Vol.18 (3), p.235-239 |
| issn | 0091-7370 1550-8080 |
| language | eng |
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| source | MEDLINE; EZB Electronic Journals Library |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Drug Contamination Fundamental and applied biological sciences. Psychology General aspects, investigation methods Hydrogen-Ion Concentration Proteins Proteins - analysis Quinolines |
| title | Protein analysis with bicinchoninic acid |
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