Response of Aequorin Bioluminescence to Rapid Changes in Calcium Concentration

@article{Hastings1969ResponseOA,
  title={Response of Aequorin Bioluminescence to Rapid Changes in Calcium Concentration},
  author={John Woodland Hastings and George Mitchell and Patrick H. Mattingly and John R. Blinks and Menno van Leeuwen},
  journal={Nature},
  year={1969},
  volume={222},
  pages={1047-1050}
}
Aequorin is a protein which emits light after reaction with calcium. The rise time and decay time of luminescence are in the millisecond region, making aequorin a useful detector of calcium in biological systems. 

Revision of the structure of the light-emitter in aequorin bioluminescence

The structure of the excited light-emitter in aequorin bioluminescence was assigned not to an amide anion of coelenteramide but to a phenolate anion on the basis of the luminescence of regenerated

Calcium Binding, Quantum Yield, and Emitting Molecule in Aequorin Bioluminescence

The extreme sensitivity to Ca2+, much more than to Sr2+, provides a basis for quick microdetermination of Ca2+ in biological fluids and has been used in detecting the relation ofCa2+ to contraction of single muscle fibres and to activity of mitochondria.

Rapid kinetic studies of the light emitting protein aequorin.

Kinetics studies of the kinetics of aequorin using stopped flow and double stopped flow apparatuses were unable to establish a Ca2+ dependence for the rate of rise of the light emission, which might be very important for delineation of the reaction mechanism.

Calcium transients in aequorin-injected frog cardiac muscle

The Ca2+-sensitive bioluminescent protein aequorin was microinjected into cells of frog at rial trabeculae to study intracellular calcium transients associated with excitation–contraction coupling.

Biochemistry of the bioluminescence of colonial hydroids and other coelenterates

The biochemical system responsible for the bioluminescent flashing in a number of coelenterates has been isolated and partially characterized and it is shown that the activity of reacted photoprotein is not restored if the calcium is removed by EDTA.

Calcium dependence of aequorin bioluminescence dissected by random mutagenesis.

Variations of luminescence kinetics, which depend on three EF hands endowed with different calcium affinities, critically determine the amplitude of aequorin responses to biological calcium signals.

Preparation and use of aequorin for rapid microdetermination of Ca 2+ in biological systems.

The photoprotein aequorin extracted from the luminescent jellyfish Aequorea aequorea offers unique advantages for detecting the presence or changes in concentration of Ca2+ in biological systems and for investigating the action of poisons such as cyanide, tetrodotoxin and so on, on biological processes12–14.
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References

SHOWING 1-6 OF 6 REFERENCES

Microdetermination of Calcium by Aequorin Luminescence

A bioluminescent protein, aequorin, isolated from the jellyfish Aequorea in dilute disodium ethylenediaminetetraacetate solution, emits light on addition specifically of Ca++ or Sr++, thus providing

Simultaneous Recording of Membrane Potential, Calcium Transient and Tension in Single Muscle Fibres

This work has simultaneously recorded changes in membrane potential, calcium transient and tension during a single contraction of an isolated muscle fibre.

FURTHER DATA ON THE BIOLUMINESCENT PROTEIN, AEQUORIN.

Apparatus for rapid and sensitive spectrophotometry.

Calcium transients in single muscle fibers.