The primary structure of histone H2B from the mollusc Patella granatina

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dc.contributor.advisorVon Holt, Claus
dc.contributor.authorVan Helden, Paul David
dc.date.accessioned2023-09-27T14:06:04Z
dc.date.available2023-09-27T14:06:04Z
dc.date.issued1978
dc.date.updated2023-09-27T14:05:41Z
dc.description.abstractHistones H2B were isolated from the gonads of a mollusc (Patella granatina) and from chicken (Gallus domesticus), crocodile (Crocodylus niloticus) and amphibian (Xenopus laevis) erythrocytes. The H2B's were purified by ion-exchange and gel exclusion chromatography. The complete primary structure of the mollusc hi stone H2B t 11 has been deduced from the sequences established of pa e a adjoining and overlapping peptides by the Edman degradation procedure. The partial structure of H2B from chicken erythrocytes (87 residues), crocodile erythrocytes (75 residues) and Xenopus erythrocytes (63 residues) was also established. The amino acid sequences are compared to those of other histones H2B. The effect of mutations on the predicted secondary structure of histone H2B is considered.
dc.identifier.apacitationVan Helden, P. D. (1978). <i>The primary structure of histone H2B from the mollusc Patella granatina</i>. (). ,Faculty of Science ,Department of Molecular and Cell Biology. Retrieved from http://hdl.handle.net/11427/38915en_ZA
dc.identifier.chicagocitationVan Helden, Paul David. <i>"The primary structure of histone H2B from the mollusc Patella granatina."</i> ., ,Faculty of Science ,Department of Molecular and Cell Biology, 1978. http://hdl.handle.net/11427/38915en_ZA
dc.identifier.citationVan Helden, P.D. 1978. The primary structure of histone H2B from the mollusc Patella granatina. . ,Faculty of Science ,Department of Molecular and Cell Biology. http://hdl.handle.net/11427/38915en_ZA
dc.identifier.ris TY - Doctoral Thesis AU - Van Helden, Paul David AB - Histones H2B were isolated from the gonads of a mollusc (Patella granatina) and from chicken (Gallus domesticus), crocodile (Crocodylus niloticus) and amphibian (Xenopus laevis) erythrocytes. The H2B's were purified by ion-exchange and gel exclusion chromatography. The complete primary structure of the mollusc hi stone H2B t 11 has been deduced from the sequences established of pa e a adjoining and overlapping peptides by the Edman degradation procedure. The partial structure of H2B from chicken erythrocytes (87 residues), crocodile erythrocytes (75 residues) and Xenopus erythrocytes (63 residues) was also established. The amino acid sequences are compared to those of other histones H2B. The effect of mutations on the predicted secondary structure of histone H2B is considered. DA - 1978 DB - OpenUCT DP - University of Cape Town KW - Biochemistry LK - https://open.uct.ac.za PY - 1978 T1 - The primary structure of histone H2B from the mollusc Patella granatina TI - The primary structure of histone H2B from the mollusc Patella granatina UR - http://hdl.handle.net/11427/38915 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/38915
dc.identifier.vancouvercitationVan Helden PD. The primary structure of histone H2B from the mollusc Patella granatina. []. ,Faculty of Science ,Department of Molecular and Cell Biology, 1978 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/38915en_ZA
dc.language.rfc3066eng
dc.publisher.departmentDepartment of Molecular and Cell Biology
dc.publisher.facultyFaculty of Science
dc.subjectBiochemistry
dc.titleThe primary structure of histone H2B from the mollusc Patella granatina
dc.typeDoctoral Thesis
dc.type.qualificationlevelDoctoral
dc.type.qualificationlevelPhD
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