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dc.contributor.advisorHarris, E. D.
dc.creatorWoodring, Stephen
dc.date.accessioned2022-06-30T16:13:50Z
dc.date.available2022-06-30T16:13:50Z
dc.date.issued1977
dc.identifier.urihttps://hdl.handle.net/1969.1/CAPSTONE-WoodringS_1977
dc.descriptionProgram year: 1976-1977en
dc.descriptionDigitized from print original stored in HDRen
dc.description.abstractLysyl oxidase from bovine ligamentum nuchae has been purified by two different methods. The first method utilized urea extraction, ion exchange chromatography, and affinity chromatography. The second method consisted of urea extraction followed by two successive runs on a Sephadex G-100 column. The different extracts were compared with respect to specific activity, copper values, and chelation effects. Significantly different results were obtained which tend to suggest the possibility of two different forms of the lysyl oxidase enzyme.en
dc.format.extent10 pagesen
dc.format.mediumelectronicen
dc.format.mimetypeapplication/pdf
dc.subjectLysyl oxidaseen
dc.subjectligamentum nuchaeen
dc.subjecturea extractionen
dc.subjectspecific activityen
dc.subjectcopper valuesen
dc.subjectchelation effectsen
dc.titleA Partial Characterization of Lysyl Oxidase from Ligamentum Nuchaeen
dc.typeThesisen
thesis.degree.departmentBiochemistry and Biophysicsen
thesis.degree.grantorUniversity Undergraduate Fellowsen
thesis.degree.levelUndergraduateen
dc.type.materialtexten


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