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dc.contributor.advisorRafael Alvarez
dc.creatorPerez-Lamigueiro, Maria A.
dc.date.accessioned2019-08-22T21:51:56Z
dc.date.available2019-08-22T21:51:56Z
dc.date.issued2004-06-01T00:00:00-07:00
dc.date.submitted2014-03-19T06:24:05-07:00
dc.identifier.urihttps://hdl.handle.net/20.500.12503/29638
dc.description.abstractPerez-Lamiguerio, Maria A., Changes in Mammalian Chromatin Structure as a Function of Protein-poly(ADP-ribosyl)ation by Endonuclease Digestion. Master of Science (Biochemistry and Molecular Biology), June 2004. 66 pages, 12 illustrations, Bibliography, 45 titles. Mammalian chromatin was exposed to either Deoxyribonuclease I or Micrococcal Nuclease digestion as a function of time of incubation and enzyme concentration. Endonuclease enzymatic reactions were stopped with EDTA. Samples were run in 1.5% agarose gels and the oligonucleosomal electrophoretic migration patterns compared. Endonuclease experiments were carried out with rat liver chromatin pre-incubated in the presence or absence of 200 μM βNAD+. A solution of 1.0 mM benzamide was used to stop enzymatic modification. The electrophoretic observations demonstrated a faster and increased degradation of chromatin when proteins were poly(ADP-ribosyl)ated prior to digestion. These results support the hypothesis that that the covalent poly(ADP-ribosyl)ation of chromatin proteins, particularly histones, induces a more relaxed structure, rendering chromatin more sensitive to endonuclease digestion.
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.subjectCell Anatomy
dc.subjectCell and Developmental Biology
dc.subjectCell Biology
dc.subjectCellular and Molecular Physiology
dc.subjectComputational Biology
dc.subjectGenetics
dc.subjectGenetics and Genomics
dc.subjectGenomics
dc.subjectLife Sciences
dc.subjectMedical Cell Biology
dc.subjectMedical Genetics
dc.subjectMedicine and Health Sciences
dc.subjectMolecular Genetics
dc.subjectOther Cell and Developmental Biology
dc.subjectOther Genetics and Genomics
dc.subjectMammalian chromatin structure
dc.subjectfunction
dc.subjectpoly(ADP-ribosyl)ation
dc.subjectendonuclease digestion
dc.subjectdeoxyribonuclease
dc.subjectmicrococcal nuclease digestion
dc.subjectenzymatic reactions
dc.subjectEDTA
dc.subjectrat liver chromatin
dc.subjectproteins
dc.subjecthistones
dc.titleChanges in Mammalian Chromatin Structure as a Function of Protein-Poly(ADP-Ribosyl)ation by Endonuclease Digestion
dc.typeThesis
thesis.degree.departmentGraduate School of Biomedical Sciences
thesis.degree.disciplineBiochemistry and Molecular Biology
thesis.degree.grantorUniversity of North Texas Health Science Center at Fort Worth
thesis.degree.nameMaster of Science
dc.contributor.committeeMemberHriday K. Das
dc.contributor.committeeMemberAlakananda Basu
dc.type.materialtext
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