新しい非筋型α-アクチニン : 肺組織に発現するα-アクチニンの構造とCa^<2+>感受性
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概要
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We have recently purified a novel nonmuscle α-actinin from chicken lung [Imamura and Masaki (1992) J. Bio1. Chem. , (1992) 267, 25927-25933. in. press]. This lung α-actinin has Ca^<2+>-sensitivity for interaction with F-actin. However, even in the presence of Ca^<2+> , its actin-gelation activity was much higher than that of Ca^<2+>-insensitive muscle-type α-actinin. Proteolytic cleavage analysis and the primary structure deduced from nucleotide sequence of cDNA showed that the lung a -actinin has structural divergence at COOH-terminal region that includes Ca^<2+>-binding EF-hand motifs. This suggests that the low Ca^<2+> -sensitivity of the lung α -actinin is ascribed to the structural divergence.
- 日本生物物理学会の論文
- 1993-03-25