Structure-function studies of mammalian purple acid phosphatases

Authors	E.G. Funhoff
Supervisors	B.A. Averill
Award date	20-02-2002
Number of pages	151
Organisations	Faculty of Science (FNWI) - Swammerdam Institute for Life Sciences (SILS)
Document type	PhD thesis
Note	Research conducted at: Universiteit van Amsterdam
Language	English
Downloads	Thesis Cover Titlepage Contents Abbreviations 1 Phosphatases 2 The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity 3 Mutational analysis of the interaction between active site residues and the loop region in mammalian purple acid phosphatases 4 Direct observation of multiple protonation states in recombinant human purple acid phosphatase 5 Probing the diiron site of human purple acid phosphatase by 1H-NMR spectroscopy 6 The Fe(III)Zn(II) form of recombinant human purple acid phosphatase is not activated by proteolysis 7 Substrate positioning by His92 is an important factor in purple acid phosphatase catalysis 8 Summary and outlook, Samenvatting Dankwoord Curriculum Vitae Stellingen behorende bij het proefschrift Cover
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