Fluorescence properties of terbium-alkaline phosphatase

A. Dean Sherry, Shun Au-Young, G. Larry Cottam

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


The addition of Tb3+ to apoalkaline phosphatase at pH 8.0 results in the formation of a metalloprotein with an enhanced Tb3+ fluorescence at 492, 545, and 580 nm. The Tb3+ excitation spectrum is most consistent with a process in which energy is transferred from one or more tyrosyl chromophores to the bound lanthanide. An analysis of the fluorescence data under equilibrium conditions yields one Tb3+ binding site per enzyme dimer with a Kn = 0.16 ± 0.02 μm. The Tb3+-alkaline phosphatase complex is not catalytically active nor does it incorporate covalently bound phosphate, but the specific activity of Zn2+-alkaline phosphatase is significantly enhanced in the presence of Tb3+ indicating that this lanthanide mimics Mg2+ in stabilizing the structure of alkaline phosphatase. The fluorescence of the Tb3+-enzyme is found to be quite sensitive to conformational changes which occur upon addition of Zn2+ or substrates.

Original languageEnglish (US)
Pages (from-to)277-282
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - Aug 1978

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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