PURIFICATION AND PARTIAL AMINO ACID SEQUENCE OF CALMODULIN FROM FUSARIUM OXYSPORUM

Abstract

Calmodulin (CaM) was purified from Fusarium oxysporum f. sp. lini SUF 402, to apparent homogeneity as judged by Tricine-SDS-polyacrylamide gel electrophoresis. Molecular mass of the isolated CaM was 18kDa and its pI was pH 4.6. Fusarium CaM had functions as an activator of rat Ca²⁺-dependent cAMP phosphodiesterase, chicken myosin light chain kinase, and rat Ca²⁺/CaM-dependent protein kinase II. The amino acid composition of Fusarium CaM was similar to those of other fungal CaM.