A circadian rhythm of the luciferin binding protein fromGonyaulax polyedra |
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| Authors: | Frank M. Sulzman Neil R. Krieger D. Van Gooch J. W. Hastings |
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| Affiliation: | (1) The Biological Laboratories, Harvard University, 02138 Cambridge, Massachusetts, USA;(2) Present address: Department of Physiology, Harvard Medical School, 02115 Boston, MA, USA;(3) Present address: Department of Pharmacology, School of Medicine, University of Pennsylvania, 19174 Philadelphia, PA, USA;(4) Present address: Division of Science and Mathematics, University of Minnesota, 56267 Morris, MN, USA |
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| Abstract: | ![]()
Summary It has previously been shown that a protein extracted fromGonyaulax polyedra strongly and specifically binds luciferin, the substrate of the bioluminescent reaction. This binding is markedly dependent on pH with tight binding at pH 8.0 and almost no binding at pH 6.5, as measured by two independent methods. A procedure for the determination of the dissociation constant (Kd) of the luciferin binding protein (LBP) is presented, and Kd is estimated to be7×10–9 M at pH 8.0, assuming an overall quantum yield of 0.1 for the bioluminescent reaction. With cells grown in a 12 h light — 12 h dark cycle, 5 to 10 times more LBP activity can be extracted from dark phase cells than from light phase cells. This rhythm persists in a circadian fashion in cultures maintained in constant dim light.Supported in part by a grant from the National Institutes of Health to J.W.H. (GM 19536) |
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