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Interaction of calmodulin with lactoferrin
Author(s) -
de Lillo A.,
Tejerina J.M.,
Fierro J.F.
Publication year - 1992
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(92)80055-l
Subject(s) - calmodulin , biotinylation , lactoferrin , affinity chromatography , agarose , binding protein , biochemistry , chemistry , enzyme , calmodulin binding proteins , calcium binding protein , calcium , microbiology and biotechnology , biology , gene , organic chemistry
Calmodulin, as a major intracellular calcium‐binding protein, regulates many Ca 2+ ‐dependent enzymes and plays an important role in a wide spectrum of cellular functions of the eukaryotes. Interaction between calmodulin and human lactoferrin, a 78 kDa protein with antibacterial properties, was found in the presence of Ca 2+ using (i) a method for the detection of calmodulin binding proteins with biotinylated calmodulin, (ii) affinity chromatography on an agarose—calmodulin column with subsequent detection by an enzyme‐linked immunosorbent assay (ELISA). The binding of calmodulin to lactoferrin blocked the ability of lactoferrin to agglutinate Micrococcus lysodeikticus .