Modified Aequorin Shows Increased Bioluminescence Activity

Abstract

Aequorin belongs to a unique class of photoproteins that emit light upon the binding of certain metals, calcium being the principal intracellular activator. This 'reporting function' of the metal-binding is instantaneous and is very easy to quantitate experimentally. The project objective was to develop a variety of recombinant forms of aequorin so they can be employed as metal biosensors. Three calcium-binding sites of aequorin were modified to examine their roles in the calcium-dependent luminescence as well as potentially binding other metal ions. Aequorins having Site 2 substitutions unexpectedly produce more light than wild-type aequorin.

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Document Details

Document Type
Technical Report
Publication Date
Aug 18, 1993
Accession Number
ADA268774

Entities

People

  • Douglas C. Prasher

Organizations

  • Woods Hole Oceanographic Institution

Tags

DTIC Thesaurus Topics

  • Amino Acids
  • Biochemistry
  • Biological Sciences
  • Biology
  • Carrier Proteins
  • Catalytic Oxidation
  • Chemical Reactions
  • Chemical Synthesis
  • Chemistry
  • Coding
  • Luminescence
  • Metals
  • Military Research
  • Molecular Biology
  • Proteins
  • Recombinant Proteins
  • Resistance

Readers

  • Cellular and Molecular Pathways of Apoptosis.
  • Computational Modeling and Simulation
  • Microbial Pathology

Technology Areas

  • Biotechnology