Kinetic studeis of human spleen adenosine deaminases

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dc.contributor.advisor Ma, Pang-Fai en_US Creazzola, Maria A. en_US 2011-06-03T19:32:11Z 2011-06-03T19:32:11Z 1978 en_US 1978
dc.identifier LD2489.Z78 1978 .C74 en_US
dc.description.abstract The hydrolysis of adenosine, 2-deoxyadenosine and 6-chloropurine riboside by adenosine deaminase preparations from human spleen has been investigated, and Km and Vm values have been determined. The effect of the substrate on the reaction velocity was followed over a 250-fold range Results showed no deviation from Michaelis-Menten kinetics. The effect of pH on Vm, Vm/Km, and the apparent activation energy was examined. Inactivation of the enzyme by p-chloromercuribenzoate suggests the involvement of one or more SH groups. Competitive inhibition by inosine and the fact that ammonia is not, an inhibitor support a reaction mechanism involving a ternary complex. The apparent activation energy of the a parameter was smaller or less sensitive to temperature than the ß parameter.Ball State UniversityMuncie, IN 47306 en_US
dc.format.extent vi, 85 leaves ; 28 cm. en_US
dc.source Virtual Press en_US
dc.subject.lcsh Adenosine deaminase. en_US
dc.subject.other Ball State University. Thesis (M.S.) en_US
dc.title Kinetic studeis of human spleen adenosine deaminases en_US Thesis (M.S.)--Ball State University. en_US
dc.identifier.cardcat-url en_US

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  • Master's Theses [5576]
    Master's theses submitted to the Graduate School by Ball State University master's degree candidates in partial fulfillment of degree requirements.

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