Human interleukin-1 receptor antagonist. High yield expression in E. coli and examination of cysteine residues.
The human IL-1 receptor antagonist (IL-1ra) was produced in a high yield E. coli expression system, and was purified in a rapid two-step purification. This recombinant IL-1ra molecule possessed full binding activity to the IL-1 receptor (type I) and totally inhibited IL-1-induced PGE2 production by...
Main Authors: | , , , , , , |
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Format: | Journal article |
Language: | English |
Published: |
1992
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_version_ | 1797081245768744960 |
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author | Steinkasserer, A Solari, R Mott, H Aplin, RT Robinson, C Willis, A Sim, R |
author_facet | Steinkasserer, A Solari, R Mott, H Aplin, RT Robinson, C Willis, A Sim, R |
author_sort | Steinkasserer, A |
collection | OXFORD |
description | The human IL-1 receptor antagonist (IL-1ra) was produced in a high yield E. coli expression system, and was purified in a rapid two-step purification. This recombinant IL-1ra molecule possessed full binding activity to the IL-1 receptor (type I) and totally inhibited IL-1-induced PGE2 production by human dermal fibroblasts. Radioalkylation and analysis of V8-derived IL-1ra peptides indicate that the four cysteines present in the IL-1ra are not disulphide-linked. |
first_indexed | 2024-03-07T01:11:52Z |
format | Journal article |
id | oxford-uuid:8d4863cf-5d83-44ab-b4f0-a1fe70429c9f |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T01:11:52Z |
publishDate | 1992 |
record_format | dspace |
spelling | oxford-uuid:8d4863cf-5d83-44ab-b4f0-a1fe70429c9f2022-03-26T22:50:16ZHuman interleukin-1 receptor antagonist. High yield expression in E. coli and examination of cysteine residues.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8d4863cf-5d83-44ab-b4f0-a1fe70429c9fEnglishSymplectic Elements at Oxford1992Steinkasserer, ASolari, RMott, HAplin, RTRobinson, CWillis, ASim, RThe human IL-1 receptor antagonist (IL-1ra) was produced in a high yield E. coli expression system, and was purified in a rapid two-step purification. This recombinant IL-1ra molecule possessed full binding activity to the IL-1 receptor (type I) and totally inhibited IL-1-induced PGE2 production by human dermal fibroblasts. Radioalkylation and analysis of V8-derived IL-1ra peptides indicate that the four cysteines present in the IL-1ra are not disulphide-linked. |
spellingShingle | Steinkasserer, A Solari, R Mott, H Aplin, RT Robinson, C Willis, A Sim, R Human interleukin-1 receptor antagonist. High yield expression in E. coli and examination of cysteine residues. |
title | Human interleukin-1 receptor antagonist. High yield expression in E. coli and examination of cysteine residues. |
title_full | Human interleukin-1 receptor antagonist. High yield expression in E. coli and examination of cysteine residues. |
title_fullStr | Human interleukin-1 receptor antagonist. High yield expression in E. coli and examination of cysteine residues. |
title_full_unstemmed | Human interleukin-1 receptor antagonist. High yield expression in E. coli and examination of cysteine residues. |
title_short | Human interleukin-1 receptor antagonist. High yield expression in E. coli and examination of cysteine residues. |
title_sort | human interleukin 1 receptor antagonist high yield expression in e coli and examination of cysteine residues |
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