Calmodulin from the water mold Achlya ambisexualis: isolation and characterization.
A protein-activator of bovine cyclic nucleotide phosphodiesterase from the water mold Achlya ambisexualis has been affinity-purified to apparent electrophoretic homogeneity. The heat-stable protein is similar in amino acid content and electrophoretic mobility on SDS acrylamide gels, to bovine brain calmodulin. It also cross-reacts with antibodies raised to the bovine protein. Achlya calmodulin activates PDE increasing its activity up to 9-fold in a Ca2+-dependent manner. The mold protein appears unusual in that its tyrosine fluorescence is unaltered by Ca2+ or by EGTA.
D000596:Amino Acids / Q000032:analysis; D002147:Calmodulin / Q000302:isolation & purification*; D005658:Fungi / Q000032:analysis* / Q000254:growth & development; D008970:Molecular Weight; D011863:Radioimmunoassay; D013050:Spectrometry, Fluorescence; D014443:Tyrosine
D000596:Amino Acids; D002147:Calmodulin; D014443:Tyrosine