Date of Award

Fall 1987

Document Type


Degree Name

Master of Science (MS)


Chemistry & Biochemistry



Committee Director

James H. Yuan

Committee Member

John D. Van Norman

Committee Member

Roy L. Williams

Committee Member

Patricia A. Pleban

Call Number for Print

Special Collections LD4331.C45H82


n-Alkylphosphates and adenosine derivatives have been observed to be competitive inhibitors of coenzyme molecules in many NAD+ requiring enzymes. In earlier studies, adenosine derivatives such as AMP, ADP and ADP-ribose were found to be coenzyme competitive inhibitors of the Lactate Dehydrogenase catalyzed reaction. However, n-alkylphosphates, to the contrary, + were found to be noncompetitive inhibitors of NAD+.

Furthermore, it was observed previously in Dr. Yuan's laboratory that the effect of n-octylphosphate on the LDH catalyzed reaction was changed from noncompetitive to competitive in the presence of low concentration of AMP. Rossmann et al. reported that the binding of adenosine region of the LDH coenzyme site is the prerequisite for the binding of the coenzyme molecule or its analogs. The purpose of synthesizing n-alkyl-ADPs is to utilize them to investigate the possible nonpolar interaction between the compound and the coenzyme binding site of rabbit muscle LDH.

The syntheses of n-alkyl-ADPs were adapted from the method described by Barker et al. for the synthesis of nucleoside phosphates and their attachment to agarose. 13C-NMR, proton NMR, FT-IR, and mass spectrometry were utilized to verify the structure of these synthetic coenzyme analogs.


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