Production of Human PTH(1-34) via a Recombinant DNA Technique
Nakagawa, S. ; Tamakashi, Y. ; Ishibashi, Y. ; Kawase, M. ; Taketomi, S. ; Nishimura, O. ; Fukuda, T.
Amsterdam : Elsevier
Amsterdam : Elsevier
| ISSN: |
0006-291X
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|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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| Topics: |
Biology
Chemistry and Pharmacology
Physics
|
| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798292263199047680 |
|---|---|
| autor | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. |
| autorsonst | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. |
| book_url | http://dx.doi.org/10.1006/bbrc.1994.1653 |
| datenlieferant | nat_lic_papers |
| fussnote | The production of hPTH(1-34) by site specific chemical cleavage of [Cys^3^5]hPTH(1-84) obtained by a biotechnology technique is described. The amino-peptide bond of S-cyanylated cysteine residues in peptides or proteins is specifically cleaved by exposure to an alkaline solution (Stark, G. R. (1977) Methods Enzymol, 47, 129-132). However, when applying this method to [Cys^3^5]hPTH(1-84), we observed many by-products. Formation of these by-products was suppressed using a short reaction in 0.03N NaOH containing 6M urea at low temperature, and hPTH(1-34) was specifically produced. The product was indistinguishable from standard hPTH(1-34) with respect to chemical and biological characterization. |
| hauptsatz | hsatz_simple |
| identnr | NLZ18346852X |
| iqvoc_descriptor_title | iqvoc_00000080:Production |
| issn | 0006-291X |
| journal_name | Biochemical and Biophysical Research Communications |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 200 (1994), S. 1735-1741 |
| search_space | articles |
| shingle_author_1 | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. |
| shingle_author_2 | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. |
| shingle_author_3 | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. |
| shingle_author_4 | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. |
| shingle_catch_all_1 | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. Production of Human PTH(1-34) via a Recombinant DNA Technique 0006-291X 0006291X Elsevier |
| shingle_catch_all_2 | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. Production of Human PTH(1-34) via a Recombinant DNA Technique 0006-291X 0006291X Elsevier |
| shingle_catch_all_3 | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. Production of Human PTH(1-34) via a Recombinant DNA Technique 0006-291X 0006291X Elsevier |
| shingle_catch_all_4 | Nakagawa, S. Tamakashi, Y. Ishibashi, Y. Kawase, M. Taketomi, S. Nishimura, O. Fukuda, T. Production of Human PTH(1-34) via a Recombinant DNA Technique 0006-291X 0006291X Elsevier |
| shingle_title_1 | Production of Human PTH(1-34) via a Recombinant DNA Technique |
| shingle_title_2 | Production of Human PTH(1-34) via a Recombinant DNA Technique |
| shingle_title_3 | Production of Human PTH(1-34) via a Recombinant DNA Technique |
| shingle_title_4 | Production of Human PTH(1-34) via a Recombinant DNA Technique |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:45:44.620Z |
| titel | Production of Human PTH(1-34) via a Recombinant DNA Technique |
| titel_suche | Production of Human PTH(1-34) via a Recombinant DNA Technique The production of hPTH(1-34) by site specific chemical cleavage of [Cys^3^5]hPTH(1-84) obtained by a biotechnology technique is described. The amino-peptide bond of S-cyanylated cysteine residues in peptides or proteins is specifically cleaved by exposure to an alkaline solution (Stark, G. R. (1977) Methods Enzymol, 47, 129-132). However, when applying this method to [Cys^3^5]hPTH(1-84), we observed many by-products. Formation of these by-products was suppressed using a short reaction in 0.03N NaOH containing 6M urea at low temperature, and hPTH(1-34) was specifically produced. The product was indistinguishable from standard hPTH(1-34) with respect to chemical and biological characterization. |
| topic | W V U |
| uid | nat_lic_papers_NLZ18346852X |