アカザラガイ・ハイブリッド・ミオシンにおける調節軽鎖の結合性

概要

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When akazara hybridized myosins prepared from akazara desensitized myosin (DM) with various molluscan and vertebrate regulatory light chains (R-LCs) were incubated in the presence of EDTA, the R-LCs were dissociated exponentially with increasing incubation period. Both the extent and rate of the dissociation were found to be considerably greater for the molluscan R-LCs than for the vertebrate R-LCs. The dissociation showed a biphasic dependence on incubation temperature. On the other hand, the fluorescence intensity of tryptophan residure in DM and of ANS bound to DM also changed biphasically. Transition temperatures for the R-LC dissociation and the fluorescence intensity were well coincided at about 20°C. It was thus strongly suggested that the molluscan R-LCs bind to DM depending on the divalent cations, whereas the vertebrate R-LCs bind largely depending on the other types of interaction. In addition, the conformational change of DM was assumed to occur above 20°C so as to ac-celexate the R-LC dissociation.
日本水産學會の論文