Date of Award

Fall 1990

Document Type


Degree Name

Master of Science (MS)


Chemistry & Biochemistry



Committee Director

Mark S. Elliot

Committee Member

Roy L. Williams

Committee Member

Laura K. Moen

Committee Member

Patricia A. Pleban

Call Number for Print

Special Collections LD4331.C45E75


The purpose of this study was to isolate and purify the enzymes, transfer RNA-guanine ribosyltrasferase and protein kinase C, and to determine whether the phosphorylating enzyme activates the insertion enzyme in vitro. Transfer RNA-guanine ribosyltransferase lost activity within several days after isolation and total, complete reactivation was accomplished in the presence of protein kinase C. This demonstrated that ribosyltransferase's instability is related to the degree of its phosphorylation. It is proposed that modification of tRNA is controlled by protein kinase C. Deactivation of the insertion enzyme leads to hypomodified tRNA which in turn is associated with neoplasia. Potential use of these results could be helpful in unraveling the mechanism of induction of cancer.


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