Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4'-dithiodipyridine
Since its introduction in 1959, Ellman's reagent (5,5'-dithio-bis(2-nitrobenzoic acid)) has been the favorite reagent for spectrophotometric measurement of protein sulfhydryls. Meanwhile however, evidence has accumulated that many protein sulfhydryls give an incomplete reaction with Ellman...
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| Published in | Analytical and bioanalytical chemistry Vol. 373; no. 4-5; pp. 266 - 276 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Germany
01.07.2002
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| Online Access | Get full text |
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| Abstract | Since its introduction in 1959, Ellman's reagent (5,5'-dithio-bis(2-nitrobenzoic acid)) has been the favorite reagent for spectrophotometric measurement of protein sulfhydryls. Meanwhile however, evidence has accumulated that many protein sulfhydryls give an incomplete reaction with Ellman's reagent, even during prolonged assay times. In the present study, the kinetic problem was solved by including cystamine as a "mediator" between the protein sulfhydryl and Ellman's reagent, as previously applied in an enzymatic thiol assay [9]. As an alternative, 4,4'-dithiodipyridine (DTDP) was used in place of Ellman's reagent. Due to its small size, amphiphilic nature, and lack of charge, DTDP quickly reacts with poorly accessible protein sulfhydryls, without any catalysis by cystamine. The DTDP method and the Ellman/cystamine method were both optimized for maximal sensitivity, minimal sample consumption (detection limit 0.2 nmol mL(-1), determination limit 0.6 nmol mL(-1)), and minimal assay time (5 min). In validation experiments, both methods gave identical results and the measured sulfhydryls/protein matched the expected values. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00216-002-1347-2. |
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| AbstractList | Since its introduction in 1959, Ellman's reagent (5,5'-dithio-bis(2-nitrobenzoic acid)) has been the favorite reagent for spectrophotometric measurement of protein sulfhydryls. Meanwhile however, evidence has accumulated that many protein sulfhydryls give an incomplete reaction with Ellman's reagent, even during prolonged assay times. In the present study, the kinetic problem was solved by including cystamine as a "mediator" between the protein sulfhydryl and Ellman's reagent, as previously applied in an enzymatic thiol assay [9]. As an alternative, 4,4'-dithiodipyridine (DTDP) was used in place of Ellman's reagent. Due to its small size, amphiphilic nature, and lack of charge, DTDP quickly reacts with poorly accessible protein sulfhydryls, without any catalysis by cystamine. The DTDP method and the Ellman/cystamine method were both optimized for maximal sensitivity, minimal sample consumption (detection limit 0.2 nmol mL(-1), determination limit 0.6 nmol mL(-1)), and minimal assay time (5 min). In validation experiments, both methods gave identical results and the measured sulfhydryls/protein matched the expected values. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00216-002-1347-2. Since its introduction in 1959, Ellman's reagent (5,5'-dithio-bis(2-nitrobenzoic acid)) has been the favorite reagent for spectrophotometric measurement of protein sulfhydryls. Meanwhile however, evidence has accumulated that many protein sulfhydryls give an incomplete reaction with Ellman's reagent, even during prolonged assay times. In the present study, the kinetic problem was solved by including cystamine as a "mediator" between the protein sulfhydryl and Ellman's reagent, as previously applied in an enzymatic thiol assay [9]. As an alternative, 4,4'-dithiodipyridine (DTDP) was used in place of Ellman's reagent. Due to its small size, amphiphilic nature, and lack of charge, DTDP quickly reacts with poorly accessible protein sulfhydryls, without any catalysis by cystamine. The DTDP method and the Ellman/cystamine method were both optimized for maximal sensitivity, minimal sample consumption (detection limit 0.2 nmol mL super(-1), determination limit 0.6 nmol mL super(-1)), and minimal assay time (5 min). In validation experiments, both methods gave identical results and the measured sulfhydryls/protein matched the expected values. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00216-002-1347-2. |
| Author | Riener, Christian K Kada, Gerald Gruber, Hermann J |
| Author_xml | – sequence: 1 givenname: Christian K surname: Riener fullname: Riener, Christian K organization: Institute of Biophysics, J. Kepler University, Altenberger Str. 69, A-4040 Linz, Austria – sequence: 2 givenname: Gerald surname: Kada fullname: Kada, Gerald – sequence: 3 givenname: Hermann J surname: Gruber fullname: Gruber, Hermann J |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12110978$$D View this record in MEDLINE/PubMed |
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| PublicationTitle | Analytical and bioanalytical chemistry |
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| Snippet | Since its introduction in 1959, Ellman's reagent (5,5'-dithio-bis(2-nitrobenzoic acid)) has been the favorite reagent for spectrophotometric measurement of... |
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| SubjectTerms | Accessibility Animals Assaying Calibration Consumption Disulfides Dithionitrobenzoic Acid Electronics Humans Mathematical analysis Muramidase - analysis Papain - analysis Proteins Proteins - analysis Proteins - standards Pyridines Reagents Reproducibility of Results Sensitivity and Specificity Serum Albumin, Bovine - analysis Servers Spectrophotometry, Ultraviolet Sulfhydryl Compounds - analysis Sulfhydryl Compounds - standards Sulfhydryl Reagents |
| Title | Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4'-dithiodipyridine |
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