アカザラガイ・ミオシンのトリニトロフェニル化〔英文〕

概要

論文の詳細を見る
When akazara scallop striated adductor myosin reacted with 2, 4, 6-trinitrobenzenesulfonate, one mol of trinitrophenyl(TNP)-group was rapidly incorporated into one mol of myosin. The amount of the TNP-group incorporated in the myosin was not influenced by the presence of 2mM sodium pyrophosphate (PPi), however, the effects of trinitrophenylation on myosin ATPase ac-tivities were remarkably affected by the presence of PPi. Thus, the Ca-ATPase activity was decreased by trinitrophenylation to 80% of its original in the absence of PPi, but to 40% in the presence of PPi. The Mg-ATPase activity both in the presence and absence of Ca2+ was increased by trinitrophen, ?? tion in the absence of PPi, maintaining a relatively high Ca2+-sensitivity. But, in the presence of PPi the activity in the absence of Ca2+ was significantly increased and that in the presence of Ca2+ was slightly decreased, losing its Ca2+-sensitivity.Both the decreased ATPase activity and Ca2+-sensitivity of TNP-myosin were found to recover by the subsequent dithiothreitol (DTT) -treatment of the myosin. Moreover, the reactivity of the SH1-type thiol of the myosin with N-(iodoacetyl)-N'-(5-sulfo-1-naphthyl)-ethylenediamine was found to be remarkably lowered by trinitrophenylation in the presence of PPi but recovered by the DTT-treatment, indicating that trinitrophenylation blocked the SH-group(s) of myosin.From these results, it is concluded that the triritrophenylation of akazara scallop myosin, especially in the presence of PPi, is accompanied by the modification of the SH-group (s) and that the modification of SH-group causes a decrease not only in myosin ATPase activity but also in Ca2+-regulating ability.
日本水産學會の論文

アカザラガイ・ミオシンのトリニトロフェニル化〔英文〕

スポンサーリンク

概要

著者

関連論文

スポンサーリンク