Tryptophan phosphorescence as a monitor of the structural role of metal ions in alkaline phosphatase

The phosphorescence properties of Trp109 in alkaline phosphatase from Escherichia coli have been utilized to probe the conformation of the polypeptide following the removal of metal ions, reconstitution with Zn2+ and Cd2+ and phosphorylation. The complete removal of metal ions induces a drastic loos...

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Veröffentlicht in:	European journal of biochemistry 1989-11, Vol.185 (3), p.573-579
Hauptverfasser:	CIONI, Patrizia, PIRAS, Luciana, STRAMBINI, Giovanni Battista
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkaline Phosphatase - isolation & purification Analytical, structural and metabolic biochemistry Binding Sites Binding, Competitive Biological and medical sciences Cadmium - analysis Enzymes and enzyme inhibitors Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Hydrolases Luminescent Measurements Magnetic Resonance Spectroscopy Metals - analysis Peptides - isolation & purification Phosphates - isolation & purification Phosphorylation Protein Conformation Spectrometry, Fluorescence Structure-Activity Relationship Tryptophan - analysis Zinc - analysis
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