Biochemical characterization of a genetically altered calmodulin in Paramecium.
Recent evidence proposes that the calcium-binding protein, calmodulin, plays a crucial role in the regulation or modulation of the calcium-dependent potassium conductance in Paramecium tetraurelia (Hinrichsen, R.D., Burgess-Cassler, A., Soltvedt, B.C., Hennessey, T. and Kung, C. (1986) Science 323, 503-506). We purified the calmodulins from both the wild type and pantophobiac A (a mutant lacking the above-mentioned conductance and whose phenotypic defect is traceable to its calmodulin) by hydrophobic interaction and immunoaffinity chromatographies, and examined them biochemically. In this paper we address the preliminary characterization of the two calmodulins and discuss the consequences of the genetic alteration. The differences described here are in their electrophoretic mobilities in polyacrylamide gel electrophoresis and in their binding characteristics to monoclonal antibodies raised against calmodulin from wild-type paramecia. Also, we present data which indicate a difference in the stimulation of the calmodulin-dependent enzyme bovine brain phosphodiesterase under certain conditions.
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D002118:Calcium / Q000502:physiology; D002147:Calmodulin / Q000502:physiology*; D004553:Electric Conductivity; D006358:Hot Temperature; D007473:Ion Channels / Q000502:physiology*; D007526:Isoelectric Point; D008970:Molecular Weight; D009154:Mutation; D010247:Paramecium / Q000502:physiology*; D013329:Structure-Activity Relationship
D000911:Antibodies, Monoclonal; D002147:Calmodulin; D007473:Ion Channels; D002118:Calcium