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Calmodulin in interferon preparations: effect of interferon on calmodulin bioactivity
Authors:P J Davis  H R Thacore  K C Chadha  W D Lawrence  J H Kite
Affiliation:1. Department of Medicine State University of New York at Buffalo School of Medicine, Veterans Administration Medical Center, Buffalo, NY 14215 USA;2. Department of Microbiology State University of New York at Buffalo School of Medicine, Veterans Administration Medical Center, Buffalo, NY 14215 USA;3. Department of Cell and Tumor Biology Roswell Park Memorial Institute Buffalo, New York 14263 USA;1. AP–HP, hôpital Raymond-Poincaré, service de médecine physique et de réadaptation, 92380 Garches, France;2. EA 4047 HANDIReSP, université Versailles – Saint-Quentin, UFR des sciences de la santé – Simone-Veil, 2, avenue de la Source-de-la-Bièvre, 78180 Montigny-Le-Bretonneux, France;1. College of Chemistry and Materials Engineering, Wenzhou University, Wenzhou, Zhejiang, 325035, China;2. Department of Chemistry and Biochemistry, University of Windsor, Windsor, ON, N9B 3P4, Canada;1. Key Laboratory of Materials for High Power Laser, Shanghai Institute of Optics and Fine Mechanics, Chinese Academy of Sciences, Shanghai 201800, PR China;2. Graduate School of Chinese Academy of Sciences, Beijing 100039, PR China
Abstract:Heat-stable calmodulin immunoreactivity and bioactivity were detected in crude preparations of various types of human, murine and chicken interferons (IFNs). Calmodulin containing HuIFN-alpha was retained on a trifluorophenothiazine-Sepharose column. The two activities were separated by serial elutions with 50 microM Ca2+ (HuIFN-alpha) followed by 2 mM EGTA (calmodulin). While maintaining its full antiviral activity, calmodulin free HuIFN-alpha inhibited enhancement of Ca2+-ATPase activity in vitro by authentic purified eukaryote calmodulin. These results indicate that IFNs are calmodulin-binding proteins and that the secretion of both IFNs and calmodulin occurs from IFN-induced cells.
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