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Calcium‐dependent binding between calmodulin and lysozyme
Author(s) -
Fierro J.F.,
Pajares M.A.,
Hardisson C.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81231-1
Subject(s) - calmodulin , lysozyme , biotinylation , affinity chromatography , calmodulin binding proteins , calcium , biochemistry , chemistry , enzyme , avidin , phosphatase , organic chemistry
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 Ca 2+ ‐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 Ca 2+ ‐calmodulin.