Metal affinity precipitation of proteins
Proteins containing multiple surface‐accessible histidine residues can be precipitated using small quantities of bis‐copper chelates. The chelates serve to crosslink the proteins, presumably via the accessible histidines, leading to the formation of large, insoluble complexes. When excess copper che...
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Online Access: | http://dx.doi.org/10.1111/j.1470-8744.1989.tb00071.x |
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crwiley:10.1111/j.1470-8744.1989.tb00071.x 2024-09-15T18:37:33+00:00 Metal affinity precipitation of proteins Van Dam, ME Wuenschell, GE Arnold, FH 1989 http://dx.doi.org/10.1111/j.1470-8744.1989.tb00071.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biotechnology and Applied Biochemistry volume 11, issue 5, page 492-502 ISSN 0885-4513 1470-8744 journal-article 1989 crwiley https://doi.org/10.1111/j.1470-8744.1989.tb00071.x 2024-08-13T04:12:34Z Proteins containing multiple surface‐accessible histidine residues can be precipitated using small quantities of bis‐copper chelates. The chelates serve to crosslink the proteins, presumably via the accessible histidines, leading to the formation of large, insoluble complexes. When excess copper chelate is used to carry out the precipitation, the resulting precipitate has a stoichiometry of 1:1 copper:accessible histidine. The precipitation is analogous to antibody‐antigen precipitin reactions and can be described qualitatively using simple equilibrium theory developed for those systems. Human hemoglobin contains a large number of surface histidines and is efficiently precipitated by the copper salt CuSO4 as well as by bis‐copper chelates. Sperm whale myoglobin contains many fewer surface histidines and is precipitated only by the bis‐chelates. The effects of the number of accessible histidines on the protein, the chain length separating the two chelates, and the pH on the precipitation reaction have been investigated. Article in Journal/Newspaper Sperm whale Wiley Online Library Biotechnology and Applied Biochemistry 11 5 492 502 |
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Wiley Online Library |
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English |
description |
Proteins containing multiple surface‐accessible histidine residues can be precipitated using small quantities of bis‐copper chelates. The chelates serve to crosslink the proteins, presumably via the accessible histidines, leading to the formation of large, insoluble complexes. When excess copper chelate is used to carry out the precipitation, the resulting precipitate has a stoichiometry of 1:1 copper:accessible histidine. The precipitation is analogous to antibody‐antigen precipitin reactions and can be described qualitatively using simple equilibrium theory developed for those systems. Human hemoglobin contains a large number of surface histidines and is efficiently precipitated by the copper salt CuSO4 as well as by bis‐copper chelates. Sperm whale myoglobin contains many fewer surface histidines and is precipitated only by the bis‐chelates. The effects of the number of accessible histidines on the protein, the chain length separating the two chelates, and the pH on the precipitation reaction have been investigated. |
format |
Article in Journal/Newspaper |
author |
Van Dam, ME Wuenschell, GE Arnold, FH |
spellingShingle |
Van Dam, ME Wuenschell, GE Arnold, FH Metal affinity precipitation of proteins |
author_facet |
Van Dam, ME Wuenschell, GE Arnold, FH |
author_sort |
Van Dam, ME |
title |
Metal affinity precipitation of proteins |
title_short |
Metal affinity precipitation of proteins |
title_full |
Metal affinity precipitation of proteins |
title_fullStr |
Metal affinity precipitation of proteins |
title_full_unstemmed |
Metal affinity precipitation of proteins |
title_sort |
metal affinity precipitation of proteins |
publisher |
Wiley |
publishDate |
1989 |
url |
http://dx.doi.org/10.1111/j.1470-8744.1989.tb00071.x |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biotechnology and Applied Biochemistry volume 11, issue 5, page 492-502 ISSN 0885-4513 1470-8744 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1470-8744.1989.tb00071.x |
container_title |
Biotechnology and Applied Biochemistry |
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11 |
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5 |
container_start_page |
492 |
op_container_end_page |
502 |
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1810481929584115712 |