Title
Essential Tyrosine Residues in Calf Liver Uridine Diphosphoglucose Pyrophosphorylase, E.C. 2.7.7.9.
Date of Award:
5-1972
Document Type:
Thesis
Degree Name:
Master of Science (MS)
Department:
Nutrition, Dietetics, and Food Sciences
Department name when degree awarded
Biochemistry
Advisor/Chair:
Roger G. Hansen
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
2293e8f32048851011d56be0c9f79e88
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. 5123.
https://digitalcommons.usu.edu/etd/5123
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