Halistaurin, phialidin and modified forms of aequorin as Ca2+ indicator in biological systems
- 15 June 1985
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 228 (3) , 745-749
- https://doi.org/10.1042/bj2280745
Abstract
Two kinds of aequorin-type photoproteins, i.e., halistaurin and phialidin, and four kinds of modified forms of aequorin, i.e., products of acetylation, ethoxycarbonylation, fluorescamine-modification and fluorescein labelling, were prepared. The modified forms of aequorin were more sensitive to Ca2+ than was aequorin in their Ca2+-triggered luminescence reactions, whereas halistaurin and phialidin were less sensitive. The emission maxima of luminescence were all within a wavelength range 450-464 nm, except for fluorescein-labelled aequorin, which emitted yellowish light (lambda max. 520 nm). A new technique of measuring Ca2+ concentration is suggested.This publication has 6 references indexed in Scilit:
- Effect of calcium chelators on the Ca2+-dependent luminescence of aequorinBiochemical Journal, 1984
- Edta-binding and acylation of the Ca2+-sensitive photoprotein aequorinFEBS Letters, 1982
- Isolation and characterization of a photoprotein, “phialidin”, and a spectrally unique green-fluorescent protein from the bioluminescent jellyfish Phialidium gregariumComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1982
- Mechanism of the luminescent intramolecular reaction of aequorinBiochemistry, 1974
- Calcium transients in single muscle fibersBiochemical and Biophysical Research Communications, 1967
- Extraction and properties of Halistaurin, a bioluminescent protein from the hydromedusan HalistauraJournal of Cellular and Comparative Physiology, 1963