CAJ | 학술논문

从丝瓜(Luffa cylindrica (L.) Roem.)卷须中纯化得到分子量为174kD的肌球蛋白,并对其进行了酶学与电子显微学的研究.这种肌球蛋白具有肌动蛋白激活的MgATPase活性,能够被抗动物肌肉的肌球蛋白的单克隆抗体识别.电子显微学研究表明:它有两个头部(大小和形状与动物肌肉的肌球蛋白相似)和一条相对较短的尾部.还对丝瓜卷须的肌动蛋白进行了观测,偶尔发现一些尾部有球状结构的肌球蛋白.该肌球蛋白的免疫特性和超微结构证明了它由2条重链组成,并与传统的肌球蛋白相似.然而,这种174 kD的肌球蛋白是否参与了丝瓜的接触卷曲有待于进一步研究.
종사과(Luffa cylindrica (L.) Roem.)권수중순화득도분자량위174kD적기구단백,병대기진행료매학여전자현미학적연구.저충기구단백구유기동단백격활적MgATPase활성,능구피항동물기육적기구단백적단극륭항체식별.전자현미학연구표명:타유량개두부(대소화형상여동물기육적기구단백상사)화일조상대교단적미부.환대사과권수적기동단백진행료관측,우이발현일사미부유구상결구적기구단백.해기구단백적면역특성화초미결구증명료타유2조중련조성,병여전통적기구단백상사.연이,저충174 kD적기구단백시부삼여료사과적접촉권곡유대우진일보연구.
The molecular structure of a higher plant myosin with two 174 kD heavy chains purified from the tendrils of Luffa cylindrica (L.) Roem. Was viewed by electron microscopy. The myosin exhibited actin-activated MgATPase activity and could be recognized immunologically by a monoclonal antibody against the skeletal muscle myosin. Electron micrographs of rotary shadowed images of this protein revealed that it had two heads with size and shape similar to those of the skeletal muscle myosin and a relatively short tail in comparison with the conventional myosin. Luffa tendril actin filaments were also visualized and occasionally other Luffa myosin-like proteins with globular structure at the tail ends were also observed. The structural similarity and immunological cross reactivity with antibodies against muscle myosin demonstrate that the 174 kD Luffa tendril myosin is a double-headed myosin. The possible involvement of myosin-actin interactions in Luffa tendril contact coiling will be the subject of further research.