Studies on heme proteins using the n.m.r. halide-ion probe technique
The n.m.r. halide probe technique is shown to be a sensitive method for detecting the binding of Cl − and Hg 2+ to proteins. The direct binding of chloride ions to proteins has been demonstrated for the first time by this technique. There appears to be only a small amount of chloride binding to hors...
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Language: | English |
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Canadian Science Publishing
1969
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Online Access: | http://dx.doi.org/10.1139/o69-025 http://www.nrcresearchpress.com/doi/pdf/10.1139/o69-025 |
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crcansciencepubl:10.1139/o69-025 2024-03-03T08:48:57+00:00 Studies on heme proteins using the n.m.r. halide-ion probe technique Ellis, William D. Dunford, H. Brian Martin, John S. 1969 http://dx.doi.org/10.1139/o69-025 http://www.nrcresearchpress.com/doi/pdf/10.1139/o69-025 en eng Canadian Science Publishing http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining Canadian Journal of Biochemistry volume 47, issue 2, page 157-163 ISSN 0008-4018 General Medicine journal-article 1969 crcansciencepubl https://doi.org/10.1139/o69-025 2024-02-07T10:53:29Z The n.m.r. halide probe technique is shown to be a sensitive method for detecting the binding of Cl − and Hg 2+ to proteins. The direct binding of chloride ions to proteins has been demonstrated for the first time by this technique. There appears to be only a small amount of chloride binding to horseradish peroxidase and to its apoprotein in basic aqueous solutions, but the binding increases markedly as the pH is lowered, indicating that the chloride is binding nonspecifically to positively charged regions on the protein. HgCl 2 was found to bind to sperm whale myoglobin in increasing amounts as the pH was raised above 7, indicating that it may be binding to regions of negative charge on the protein. Use of the halide-ion probe technique as a means of detection of reactive sulfhydryl groups by HgCl 2 titration led to the finding that there is one reactive sulfhydryl group in peroxidase, and that the rotational correlation time for the peroxidase–HgCl 2 complex may be caused by rotation of the segment of the protein containing the sulfhydryl group rather than rotation of the entire protein. One sulfhydryl group was detected in bovine hemoglobin and possibly a second sulfhydryl group of lower activity. Article in Journal/Newspaper Sperm whale Canadian Science Publishing Canadian Journal of Biochemistry 47 2 157 163 |
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Open Polar |
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Canadian Science Publishing |
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crcansciencepubl |
language |
English |
topic |
General Medicine |
spellingShingle |
General Medicine Ellis, William D. Dunford, H. Brian Martin, John S. Studies on heme proteins using the n.m.r. halide-ion probe technique |
topic_facet |
General Medicine |
description |
The n.m.r. halide probe technique is shown to be a sensitive method for detecting the binding of Cl − and Hg 2+ to proteins. The direct binding of chloride ions to proteins has been demonstrated for the first time by this technique. There appears to be only a small amount of chloride binding to horseradish peroxidase and to its apoprotein in basic aqueous solutions, but the binding increases markedly as the pH is lowered, indicating that the chloride is binding nonspecifically to positively charged regions on the protein. HgCl 2 was found to bind to sperm whale myoglobin in increasing amounts as the pH was raised above 7, indicating that it may be binding to regions of negative charge on the protein. Use of the halide-ion probe technique as a means of detection of reactive sulfhydryl groups by HgCl 2 titration led to the finding that there is one reactive sulfhydryl group in peroxidase, and that the rotational correlation time for the peroxidase–HgCl 2 complex may be caused by rotation of the segment of the protein containing the sulfhydryl group rather than rotation of the entire protein. One sulfhydryl group was detected in bovine hemoglobin and possibly a second sulfhydryl group of lower activity. |
format |
Article in Journal/Newspaper |
author |
Ellis, William D. Dunford, H. Brian Martin, John S. |
author_facet |
Ellis, William D. Dunford, H. Brian Martin, John S. |
author_sort |
Ellis, William D. |
title |
Studies on heme proteins using the n.m.r. halide-ion probe technique |
title_short |
Studies on heme proteins using the n.m.r. halide-ion probe technique |
title_full |
Studies on heme proteins using the n.m.r. halide-ion probe technique |
title_fullStr |
Studies on heme proteins using the n.m.r. halide-ion probe technique |
title_full_unstemmed |
Studies on heme proteins using the n.m.r. halide-ion probe technique |
title_sort |
studies on heme proteins using the n.m.r. halide-ion probe technique |
publisher |
Canadian Science Publishing |
publishDate |
1969 |
url |
http://dx.doi.org/10.1139/o69-025 http://www.nrcresearchpress.com/doi/pdf/10.1139/o69-025 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Canadian Journal of Biochemistry volume 47, issue 2, page 157-163 ISSN 0008-4018 |
op_rights |
http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining |
op_doi |
https://doi.org/10.1139/o69-025 |
container_title |
Canadian Journal of Biochemistry |
container_volume |
47 |
container_issue |
2 |
container_start_page |
157 |
op_container_end_page |
163 |
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1792506007624089600 |