Structure/Function Relationships in Human Phenylalanine Hydroxylase. Effect of Terminal Deletions on the Oligomerization, Activation and Cooperativity of Substrate Binding to the Enzyme
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1996.0813r.x/fullpdf
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1. The activation of rat liver phenylalanine hydroxylase by limited proteolysis, lysolecithin, and tocopherol phosphate. Changes in conformation and catalytic properties.
2. Hydrophobic C-terminal amino acids in the .beta.-subunit are involved in assembly with the .alpha.-subunit of sodium-potassium-ATPase
3. Single-Site Mutations in the C-Terminal Domain of Bacteriophage .lambda. cI Repressor Alter Cooperative Interactions between Dimers Adjacently Bound to OR
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