Abstract
Isolated cell wall preparations of N. crassa bind significant levels of Ca, Mg and other divalent cations. Enzymatic treatment of the cell wall with beta-(1,3)-glucanase, but not with chitinase, resulted in solubilization of only the calcium-binding protein fraction. A calcium-binding protein (CaBP) was purified by metal-chelate affinity chromatography and reversed phase HPLC. CaBP has an Mr of around 6 kDa on SDS-PAGE and mass spectrometry showed that it has a molecular mass of 5744 Da. One mole of CaBP binds 2 moles of calcium and is partially inhibited (15-50%) by other divalent cations (Mg, Ni and Cu). Quenching of tryptophan fluorescence was observed upon copper binding but not calcium binding. This is a first report of a calcium binding protein from the cell wall of fungi.
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