Calcium-dependent binding between calmodulin and lysozyme.
Calmodulin, an acidic protein that binds calcium with high affinity, has multiple roles in the activation of many enzymes involved in cellular regulation of eukaryotes. In this study we show that calmodulin binding to hen egg-white lysozyme, in a Ca2+-dependent way, was observed using electroblots incubated with biotinylated calmodulin and detected with avidin-alkaline phosphatase or for affinity chromatography on a gel calmodulin column. Antimicrobial activity of lysozyme was not modified in the presence of Ca2+-calmodulin.
Fierro
J F
JF
Departamento de Biologia Funcional, Facultad de Medicina, Universidad de Oviedo, Spain.
Pajares
M A
MA
Hardisson
C
C
D000469:Alkaline Phosphatase; D001360:Avidin; D001710:Biotin; D002118:Calcium / Q000494:pharmacology*; D002147:Calmodulin / Q000378:metabolism* / Q000494:pharmacology; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D008837:Micrococcus / Q000378:metabolism; D009113:Muramidase / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects
D002147:Calmodulin; D001360:Avidin; D001710:Biotin; D000469:Alkaline Phosphatase; D009113:Muramidase; D002118:Calcium