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Efficiency of apophotoprotein charging depends strongly on protein concentration Eugene S. Vysotski*; Ludmila A. Frank; Vladimir S. Bondar Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk 660036, Russia      *(vys@bmbiris.bmb.uga.edu) Apoobelin and apoaequorin charging with coelenterazine was investigated for apoprotein concentrations in the range from 10-10 to 10-5 M. The efficiency of the yield of the protein charged with coelenterazine increases as the concentration of the apophotoprotein increases. The yield of active photoproteins is approximately 20 times higher at 10-5 than at 10-10 M concentration of apophotoprotein. Coelenterazine concentration increase does not enhance the yield of active photoprotein. On the contrary, the high molar abundance of coelenterazine decreases the yield of charged photoprotein. A mathematical model describing the process of coelenterazine binding is suggested. Using this model the apparent dissociation constant for coelenterazine was calculated. Kd for obelin and aequorin is 6x10-7 and 8x10-7 M respectively. The low value of the apparent dissociation constant suggests that the photoprotein complex is stable, this, strictly speaking, being observed in reality. This observation has to be taken into account in the estimation of gene expression using the light response from cells expressing photoprotein. Supported by Bayer AG (Germany). [Poster: vysotski.eugene.25131]

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