PURIFICATION AND PARTIAL AMINO ACID SEQUENCE OF CALMODULIN FROM FUSARIUM OXYSPORUM

TAMOTSU HOSHINO; AKIHIRO MIZUTANI; TAKUJI SASAKI; HIROYOSHI HIDAKA; TUNEO YAMANE

doi:10.2323/jgam.40.43

PURIFICATION AND PARTIAL AMINO ACID SEQUENCE OF CALMODULIN FROM FUSARIUM OXYSPORUM

TAMOTSU HOSHINO, AKIHIRO MIZUTANI, TAKUJI SASAKI, HIROYOSHI HIDAKA, TUNEO YAMANE

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ジャーナルフリー

1994 年 40 巻 1 号 p. 43-51

DOI https://doi.org/10.2323/jgam.40.43

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抄録

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.

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