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The importance of N-linked glycosylation on the N-domain of angiotensin-I converting enzyme
Angiotensin-I converting enzyme (ACE) is an important drug target in the treatment of heart disease due to its role in the regulation of blood pressure. ACE contains two domains, the N- and C-domains, both of which are catalytically active and heavily glycosylated. Glycosylation is one of the most i...
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| Format: | Thesis |
| Language: | English |
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Division of Medical Biochemistry
2014
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| _version_ | 1867613325680967680 |
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| access_status_str | Open Access |
| author | Anthony, Colin Scott |
| author2 | Sturrock, Edward D |
| author_browse | Anthony, Colin Scott Sturrock, Edward D |
| author_facet | Sturrock, Edward D Anthony, Colin Scott |
| author_sort | Anthony, Colin Scott |
| collection | Thesis |
| description | Angiotensin-I converting enzyme (ACE) is an important drug target in the treatment of heart disease due to its role in the regulation of blood pressure. ACE contains two domains, the N- and C-domains, both of which are catalytically active and heavily glycosylated. Glycosylation is one of the most important forms of post-translational modification, having a wide range of functions including protein folding, modulation of the immune response, and providing targeting signals. Glycosylation is required for the expression of active ACE and structural studies of ACE have been fraught with severe difficulties because of surface N-glycosylation of the protein. This problem has been addressed to a large extent with respect to the C-domain, where the role of glycosylation has been extensively characterised and a minimally glycosylated form was able to crystallise reproducibly. As yet, little is known about the degree and importance of N-linked glycosylation on the N-domain. The generation of minimally glycosylated N-domain, however, requires a greater understanding of the relative importance of the individual N-linked glycosylation sites. |
| format | Thesis |
| id | oai:open.uct.ac.za:11427/10051 |
| institution | University of Cape Town (South Africa) |
| language | eng |
| last_indexed | 2026-06-10T12:34:20.437Z |
| license_str | Not specified — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository |
| publishDate | 2014 |
| publishDateRange | 2014 |
| publishDateSort | 2014 |
| publisher | Division of Medical Biochemistry |
| publisherStr | Division of Medical Biochemistry |
| record_format | dspace |
| source_str | UCTD — University of Cape Town Open Access Repository |
| spelling | oai:open.uct.ac.za:11427/10051 The importance of N-linked glycosylation on the N-domain of angiotensin-I converting enzyme Anthony, Colin Scott Sturrock, Edward D Medical Biochemistry Angiotensin-I converting enzyme (ACE) is an important drug target in the treatment of heart disease due to its role in the regulation of blood pressure. ACE contains two domains, the N- and C-domains, both of which are catalytically active and heavily glycosylated. Glycosylation is one of the most important forms of post-translational modification, having a wide range of functions including protein folding, modulation of the immune response, and providing targeting signals. Glycosylation is required for the expression of active ACE and structural studies of ACE have been fraught with severe difficulties because of surface N-glycosylation of the protein. This problem has been addressed to a large extent with respect to the C-domain, where the role of glycosylation has been extensively characterised and a minimally glycosylated form was able to crystallise reproducibly. As yet, little is known about the degree and importance of N-linked glycosylation on the N-domain. The generation of minimally glycosylated N-domain, however, requires a greater understanding of the relative importance of the individual N-linked glycosylation sites. 2014-12-26T06:18:48Z 2014-12-26T06:18:48Z 2011 Doctoral Thesis Doctoral PhD http://hdl.handle.net/11427/10051 eng application/pdf Division of Medical Biochemistry Faculty of Health Sciences University of Cape Town |
| spellingShingle | Medical Biochemistry Anthony, Colin Scott The importance of N-linked glycosylation on the N-domain of angiotensin-I converting enzyme |
| thesis_degree_str | Doctoral |
| title | The importance of N-linked glycosylation on the N-domain of angiotensin-I converting enzyme |
| title_full | The importance of N-linked glycosylation on the N-domain of angiotensin-I converting enzyme |
| title_fullStr | The importance of N-linked glycosylation on the N-domain of angiotensin-I converting enzyme |
| title_full_unstemmed | The importance of N-linked glycosylation on the N-domain of angiotensin-I converting enzyme |
| title_short | The importance of N-linked glycosylation on the N-domain of angiotensin-I converting enzyme |
| title_sort | importance of n linked glycosylation on the n domain of angiotensin i converting enzyme |
| topic | Medical Biochemistry |
| url | http://hdl.handle.net/11427/10051 |
| work_keys_str_mv | AT anthonycolinscott theimportanceofnlinkedglycosylationonthendomainofangiotensiniconvertingenzyme AT anthonycolinscott importanceofnlinkedglycosylationonthendomainofangiotensiniconvertingenzyme |