ADDITIONAL CHARACTERIZATION OF ADENOSINE NUCLEOSIDASE FROM ALASKA PEA SEEDS

dc.contributor.advisorKline, Paul
dc.contributor.authorAlruwaili, Awatif Hanif
dc.contributor.committeememberBurden, Donald
dc.contributor.committeememberMiller, Justin
dc.contributor.departmentChemistryen_US
dc.date.accessioned2017-10-04T20:13:28Z
dc.date.available2017-10-04T20:13:28Z
dc.date.issued2017-04-17
dc.description.abstractAdenosine 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.abstractThe 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.description.degreeM.S.
dc.identifier.urihttp://jewlscholar.mtsu.edu/xmlui/handle/mtsu/5382
dc.publisherMiddle Tennessee State University
dc.subject.umiChemistry
dc.thesis.degreegrantorMiddle Tennessee State University
dc.thesis.degreelevelMasters
dc.titleADDITIONAL CHARACTERIZATION OF ADENOSINE NUCLEOSIDASE FROM ALASKA PEA SEEDS
dc.typeThesis

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