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ADDITIONAL CHARACTERIZATION OF ADENOSINE NUCLEOSIDASE FROM ALASKA PEA SEEDS

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dc.contributor.advisor Kline, Paul
dc.contributor.author Alruwaili, Awatif Hanif
dc.date.accessioned 2017-10-04T20:13:28Z
dc.date.available 2017-10-04T20:13:28Z
dc.date.issued 2017-04-17
dc.identifier.uri http://jewlscholar.mtsu.edu/xmlui/handle/mtsu/5382
dc.description.abstract Adenosine nucleosidase was purified from Alaska pea seeds six days after germination. A 3-fold purification has been reached with a 0.56 % recovery. The purification scheme involved ammonium sulfate precipitation between 30% and 60% saturation, followed by ion exchange chromatography on a DEAE column. A final chromatography step used a hydroxyapatite column. The subunit molecular weight of adenosine nucleosidase was determined by SDS-PAGE to be 26.7 kD. The Michaelis constant, Km, and the maximum velocity, V max, for inosine were determined to be 377.7 141.7 M and 0.00078 0.000106 M/min respectively.
dc.description.abstract The substrate specificity of the enzyme was investigated using 2’-deoxyinosine, allopurinol riboside, 3-deazauridine, and adenine- β-arabinofuranoside. Based on the observed substrate specificity, adenosine nucleosidase from Alaska pea seeds hydrolyzes both purines and pyrimidines. While these results place adenosine nucleosidase in the non-specific inosine-uridine nucleoside hydrolases (IU-NH), significant differences in its substrate specificity compared to the lead enzyme of the class, (IU-NH) from Crithidia fasciculata were found.
dc.publisher Middle Tennessee State University
dc.title ADDITIONAL CHARACTERIZATION OF ADENOSINE NUCLEOSIDASE FROM ALASKA PEA SEEDS
dc.type Thesis
dc.contributor.committeemember Burden, Donald
dc.contributor.committeemember Miller, Justin
dc.thesis.degreelevel Masters
dc.thesis.degreegrantor Middle Tennessee State University
dc.subject.umi Chemistry
dc.description.degree M.S.
dc.contributor.department Chemistry en_US


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