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CHARACTERIZATION OF ADENOSINE NUCLEOSIDASE FROM ALASKA PEA SEEDS

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dc.contributor.advisor kline, paul en_US
dc.contributor.author Shamsuddin, Abdullah Khairuddin en_US
dc.date.accessioned 2015-08-25T14:38:57Z
dc.date.available 2015-08-25T14:38:57Z
dc.date.issued 2015-06-22 en_US
dc.identifier.uri http://jewlscholar.mtsu.edu/handle/mtsu/4539
dc.description.abstract Adenosine nucleosidase was purified from Alaska pea seeds five days after germination. A 4-fold purification has been reached with a 1.3 % recovery. The subunit molecular weight of adenosine nucleosidase was determined by mass spectrometry to be 26,103 daltons. The number of subunits was 1. The Michaelis constant, Km, and the maximum velocity, V max, for adenosine were determined to be 137 48 M, and 0.34 0.02 M/min respectively. en_US
dc.description.abstract In addition, the substrate specificity of the enzyme was investigated. Based on the observed substrate specificity, adenosine nucleosidase from Alaska pea seeds belongs to the non-specific inosine-uridine nucleoside hydrolases (IU-NHs). An interesting finding was the fact that the purified enzyme was the only plant source that used 2, 3, and 5-deoxyadenosine as substrates. This is completely different from the parasitic protozoa IU-NH, specifically the nucleoside hydrolase from C. fasciculata, which showed no activity toward deoxynucleosides. This difference also indicates that adenosine nucleosidase from Alaska pea goes through a different mechanism of reaction from that of parasitic protozoa. While these results provide insight about the enzyme from Alaska pea seeds, further conformation is required to support the statements above. en_US
dc.publisher Middle Tennessee State University en_US
dc.subject Adenosine nucleosidase en_US
dc.subject Characterization en_US
dc.subject Nucleoside hydrolases en_US
dc.subject Purification en_US
dc.subject Substrate specificity en_US
dc.title CHARACTERIZATION OF ADENOSINE NUCLEOSIDASE FROM ALASKA PEA SEEDS en_US
dc.type Thesis en_US
dc.contributor.committeemember burden, donald en_US
dc.contributor.committeemember bicker, kevin en_US
dc.thesis.degreelevel Masters en_US
dc.thesis.degreegrantor Middle Tennessee State University en_US
dc.subject.umi Chemistry en_US
dc.description.degree M.S. en_US
dc.contributor.department Chemistry en_US


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