Full Text Available
Note: Clicking the button above will open the full text document at the original institutional repository in a new window.
The present thesis looks at the behaviour of internalised cell surface-derived membrane marker in comparison with the behaviour of endocytosed HRP (horse-radish peroxidase) as a fluid-phase contents marker. The pooling and/or segregation in the endosome was measured by determining co-localization wi...
| Main Author: | |
|---|---|
| Other Authors: | |
| Format: | Thesis |
| Language: | English |
| Published: |
Division of Biomedical Engineering
2018
|
| Subjects: | |
| Tags: |
No Tags, Be the first to tag this record!
|
| _version_ | 1867613150233231360 |
|---|---|
| access_status_str | Open Access |
| author | Legalatladi, Seetsela |
| author2 | Thilo, Lutz |
| author_browse | Legalatladi, Seetsela Thilo, Lutz |
| author_facet | Thilo, Lutz Legalatladi, Seetsela |
| author_sort | Legalatladi, Seetsela |
| collection | Thesis |
| description | The present thesis looks at the behaviour of internalised cell surface-derived membrane marker in comparison with the behaviour of endocytosed HRP (horse-radish peroxidase) as a fluid-phase contents marker. The pooling and/or segregation in the endosome was measured by determining co-localization with HRP. Colocalization of the two markers in the endosome is studied by using the ability of HRP to catalyse the crosslinking of membrane marker in endosomes with DAB (3,3'-diaminobenzidine), rendering the membrane marker detergent insoluble. To study the kinetic behaviour of membrane marker, radioactive galactose was covalently bound to cell-surface glycoconjugates on mouse macrophage-cells, P388D₁, as catalysed by galactosyltransferase. This provided a general membrane marker. After endocytosis-derived redistribution of membrane marker between the cell surface and endosomal membrane, a steady state was established with about 16% of the label on internal membranes. The bulk of the label on the cell surface was removable by subsequent treatment with β-galactosidase. |
| format | Thesis |
| id | oai:open.uct.ac.za:11427/27047 |
| institution | University of Cape Town (South Africa) |
| language | eng |
| last_indexed | 2026-06-10T12:31:34.243Z |
| license_str | Not specified — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository |
| publishDate | 2018 |
| publishDateRange | 2018 |
| publishDateSort | 2018 |
| publisher | Division of Biomedical Engineering |
| publisherStr | Division of Biomedical Engineering |
| record_format | dspace |
| source_str | UCTD — University of Cape Town Open Access Repository |
| spelling | oai:open.uct.ac.za:11427/27047 The kinetics of endosome processing Legalatladi, Seetsela Thilo, Lutz Biomedical Engineering Endocytosis Endosomes Biological transport The present thesis looks at the behaviour of internalised cell surface-derived membrane marker in comparison with the behaviour of endocytosed HRP (horse-radish peroxidase) as a fluid-phase contents marker. The pooling and/or segregation in the endosome was measured by determining co-localization with HRP. Colocalization of the two markers in the endosome is studied by using the ability of HRP to catalyse the crosslinking of membrane marker in endosomes with DAB (3,3'-diaminobenzidine), rendering the membrane marker detergent insoluble. To study the kinetic behaviour of membrane marker, radioactive galactose was covalently bound to cell-surface glycoconjugates on mouse macrophage-cells, P388D₁, as catalysed by galactosyltransferase. This provided a general membrane marker. After endocytosis-derived redistribution of membrane marker between the cell surface and endosomal membrane, a steady state was established with about 16% of the label on internal membranes. The bulk of the label on the cell surface was removable by subsequent treatment with β-galactosidase. 2018-01-29T07:13:44Z 2018-01-29T07:13:44Z 1995 Master Thesis Masters MSc (Med) http://hdl.handle.net/11427/27047 eng application/pdf Division of Biomedical Engineering Faculty of Health Sciences University of Cape Town |
| spellingShingle | Biomedical Engineering Endocytosis Endosomes Biological transport Legalatladi, Seetsela The kinetics of endosome processing |
| thesis_degree_str | Master's |
| title | The kinetics of endosome processing |
| title_full | The kinetics of endosome processing |
| title_fullStr | The kinetics of endosome processing |
| title_full_unstemmed | The kinetics of endosome processing |
| title_short | The kinetics of endosome processing |
| title_sort | kinetics of endosome processing |
| topic | Biomedical Engineering Endocytosis Endosomes Biological transport |
| url | http://hdl.handle.net/11427/27047 |
| work_keys_str_mv | AT legalatladiseetsela thekineticsofendosomeprocessing AT legalatladiseetsela kineticsofendosomeprocessing |