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dc.contributor.advisorMorgan, David G.
dc.contributor.authorThall, Aron D.
dc.date.accessioned2011-08-01T19:22:56Z
dc.date.available2011-08-01T19:22:56Z
dc.date.issued1982
dc.identifier.urihttp://hdl.handle.net/10920/22976
dc.description18 p.en_US
dc.description.abstractThe project was to develop a procedure which would enable a rapid and efficient measurement of the purity of dopamine. The procedure was designed to determine how much of the dopamine originally present in a tissue homogenate buffer solution remained as a function of time and was specifically designed for a receptor binding assay involving dopamine as a ligand. It involved the stabilization of tritiated dopamine by acetylation and its isolation by extraction. The purity of tritiated dopamine was found to decrease by 2% during the duration of the receptor binding assay. Ascorbic acid. a potent antioxidant. had no effect on the purity decrease of dopamine in the homogenate.en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen_US
dc.publisherKalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Biology Senior Individualized Projects Collection
dc.relation.ispartofseriesSenior Individualized Projects. Biology;
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.
dc.titleDegradation of Striatal Dopamine in Tissue Extracts Taken from C3He/J Miceen_US
dc.typeThesisen_US
KCollege.Access.ContactIf you are not a current Kalamazoo College student, faculty, or staff member, email dspace@kzoo.edu to request access to this thesis.


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  • Biology Senior Individualized Projects [1549]
    This collection includes Senior Individualized Projects (SIP's) completed in the Biology Department. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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