Date of Award:
5-1972
Document Type:
Thesis
Degree Name:
Master of Science (MS)
Department:
Chemistry and Biochemistry
Committee Chair(s)
Roger G. Hansen
Committee
Roger G. Hansen
Committee
Richard C. Anderson
Committee
Thomas M. Farley
Committee
Thomas Emery
Committee
Bruce F. Burnham
Abstract
The catalytic necessity of tyrosine residues in uridine diphospho- glucose pyrophosphorylase [E.C. 2.7.7.9] was investigated. Chemical modification of the pyrophosphorylase by N-acetylimidazole indicated that tyrosine residues were essential for activity. Approximately 23 of 112 tyrosines per molecule of 475,000 Daltons could be 0-acetylated. Solvent perturbation difference spectroscopy supported this number of exposed tyrosine side chains and in conjunction with chemical modification indicated that at least 11 to 12 tyrosyl residues per protein molecule are fully exposed. it her subst rate, uridine t riphosphate or uridine diphosphoglucose, afforded significant protection against inactivation by N-acetylimidazole.
The significance of these tyrosine residues is discussed in terms of a quaternary subunit model for uridine diphosphoglucose pyrophosphorylase.
Checksum
fe31c21b743348a0936147d860d9f5a5
Recommended Citation
Bachmann, Robert Carl, "Essential Tyrosine Residues in Calf Liver Uridine Diphosphoglucose Pyrophosphorylase, E.C. 2.7.7.9." (1972). All Graduate Theses and Dissertations, Spring 1920 to Summer 2023. 5123.
https://digitalcommons.usu.edu/etd/5123
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