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PMID: 238624 Published · ppublish English Journal Article

Comparative aspects of the calcium-sensitive photoproteins aequorin and obelin.

Biochimica et biophysica acta ·Vol. 396 ·No. 1 ·1975-07-08 ·Pages 133-40

Moisescu DG, Ashley CC, Campbell AK

Abstract

1. The calcium-dependency of the process of light emission has been investigated for the photoproteins aequorin and obelin. 2. The experimental curves of light production, expressed as a percentage of the maximal rate of utilisation, versus pCa are accurately predicted by the cooperative action of at least 2Ca-2+ for aequorin and at least 3Ca-2+ for obelin. 3. At low total monovalent cation concentrations, a pH change from 6.8 to 7.1 shifts the light production vs pCa curve by approx. 0.2 pCa units to the right for aequorin, while that for obelin is shifted by some 0.37 pCa units. 4. Other monovalent cations, such as Na+ are able to compete with Ca-2+ for the active sites of aequorin and also shift the light production vs pCa curve to the right. There is no apparent change in the calcium stoichiometry for light production under these conditions. 5. The same calcium stoichiometry for light emission was also obtained for aequorin or obelin in the presence of either unbuffered Ca-2+ solutions or of calcium/EGTA buffers.

MeSH Terms
Aequorin Animals Binding Sites Calcium Cnidaria Egtazic Acid Hydrogen-Ion Concentration Kinetics Light Luminescent Proteins Mathematics Osmolar Concentration Protein Binding Proteins Sodium
Chemicals
Luminescent Proteins Proteins obelin Aequorin Egtazic Acid Sodium Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Moisescu D G
Ashley C C
Campbell A K
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1975-07-08
Pages
133-40
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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