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Bibliography: leaves 207-233.
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| Format: | Thesis |
| Language: | English |
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Department of Molecular and Cell Biology
2015
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| _version_ | 1867613282678865920 |
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| access_status_str | Open Access |
| author | De Groot, Petronella Christina |
| author2 | Von Holt, Claus |
| author_browse | De Groot, Petronella Christina Von Holt, Claus |
| author_facet | Von Holt, Claus De Groot, Petronella Christina |
| author_sort | De Groot, Petronella Christina |
| collection | Thesis |
| description | Bibliography: leaves 207-233. |
| format | Thesis |
| id | oai:open.uct.ac.za:11427/15667 |
| institution | University of Cape Town (South Africa) |
| language | eng |
| last_indexed | 2026-06-10T12:33:40.116Z |
| license_str | Not specified — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository |
| publishDate | 2015 |
| publishDateRange | 2015 |
| publishDateSort | 2015 |
| publisher | Department of Molecular and Cell Biology |
| publisherStr | Department of Molecular and Cell Biology |
| record_format | dspace |
| source_str | UCTD — University of Cape Town Open Access Repository |
| spelling | oai:open.uct.ac.za:11427/15667 The histone H1 of the sea urchin embryo, partial structures, enzymatic modifactions and developmental programme De Groot, Petronella Christina Von Holt, Claus Strickland, W N Biochemistry Bibliography: leaves 207-233. Developmental biology owes a tremendous debt to sea urchins. These animals have proved to be experimental jewels, and since they are distributed abundantly along the Peninsula coastline, they are readily at hand. Sea urchin embryos have been shown to be extremely well suited for analysis of developmental processes at the ultrastructural, biochemical and molecular levels. This project is a study of the very lysine-rich histone fraction or H1-histone fraction of Parechinus angulosus embryo. The first part deals with the characterization and separation of the H1-variants present in the late gastrula embryo. The second part describes the determination of the partial primary structure of the three chromatographically separated H1-fractions: The amino acid composition and sequences of the H1-histone variants are compared to those of H1-histones from other sea urchin embryo species and from various other sources. The third part is a study of the histone variant synthesis program during the early development. [3H] Lysine incorporation into newly synthesized histones was utilized to examine the histone synthetic program. This part also describes the examination of histone acetylation and phosphorylation occurring during the ninth cell cycle of development. Examination of the modification of the different histone variants and modifications of the histone variants at the different cell stages are discussed. 2015-12-08T06:56:45Z 2015-12-08T06:56:45Z 1982 Master Thesis Masters MSc http://hdl.handle.net/11427/15667 eng application/pdf Department of Molecular and Cell Biology Faculty of Science University of Cape Town |
| spellingShingle | Biochemistry De Groot, Petronella Christina The histone H1 of the sea urchin embryo, partial structures, enzymatic modifactions and developmental programme |
| thesis_degree_str | Master's |
| title | The histone H1 of the sea urchin embryo, partial structures, enzymatic modifactions and developmental programme |
| title_full | The histone H1 of the sea urchin embryo, partial structures, enzymatic modifactions and developmental programme |
| title_fullStr | The histone H1 of the sea urchin embryo, partial structures, enzymatic modifactions and developmental programme |
| title_full_unstemmed | The histone H1 of the sea urchin embryo, partial structures, enzymatic modifactions and developmental programme |
| title_short | The histone H1 of the sea urchin embryo, partial structures, enzymatic modifactions and developmental programme |
| title_sort | histone h1 of the sea urchin embryo partial structures enzymatic modifactions and developmental programme |
| topic | Biochemistry |
| url | http://hdl.handle.net/11427/15667 |
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