Isolation and purification of calmodulin from the shrimp, Crangon crangon.
Calmodulin was isolated and purified from shrimp abdominal muscle by heat precipitation, ion exchange and hydrophobic interaction chromatography. The purified calmodulin was homogeneous when evaluated by polyacrylamide gel electrophoresis. A still remaining contaminant was eliminated by high performance liquid chromatography on a phenyl column. The biological and physicochemical properties of shrimp calmodulin such as amino acid composition, molecular weight and the ability to activate calmodulin-deficient bovine heart phosphodiesterase were compared to those of other invertebrate calmodulins.
Michael
R H
RH
Universität Oldenburg, Dept. Zoophysiology, Germany.
Pipkorn
R
R
Willig
A
A
Jaros
P P
PP
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002147:Calmodulin / Q000737:chemistry / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D033364:Decapoda / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D008970:Molecular Weight
D000596:Amino Acids; D002147:Calmodulin; D015105:3',5'-Cyclic-AMP Phosphodiesterases