为了方便工业界和商贸领域,选用不同厂家生产的PTT-PET自卷曲长丝制作成绞丝,根据之前筛选的最佳热处理工艺,设计了数种方法计算绞丝弹性伸长率,与相同热处理后的单根长丝弹性及成熟工艺制造的织物弹性进行相关性分析,确定出一种快速准...为了方便工业界和商贸领域,选用不同厂家生产的PTT-PET自卷曲长丝制作成绞丝,根据之前筛选的最佳热处理工艺,设计了数种方法计算绞丝弹性伸长率,与相同热处理后的单根长丝弹性及成熟工艺制造的织物弹性进行相关性分析,确定出一种快速准确的自卷曲丝弹性测试方法:绞丝经120℃干热处理8 min后测试负荷—伸长曲线;负荷—伸长曲线上以0.010 c N/dtex应力下的横坐标作为弹力起始点,以平行于断裂点与起始点连线的直线与拉伸曲线的切点作为弹力终点,计算弹性伸长率所需的绞丝弹性伸长量为起始点与终结点之间的伸长,绞丝原长为起始点对应的绞丝长度,测试绞数为10绞。展开更多
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 MgATP...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.展开更多
文摘为了方便工业界和商贸领域,选用不同厂家生产的PTT-PET自卷曲长丝制作成绞丝,根据之前筛选的最佳热处理工艺,设计了数种方法计算绞丝弹性伸长率,与相同热处理后的单根长丝弹性及成熟工艺制造的织物弹性进行相关性分析,确定出一种快速准确的自卷曲丝弹性测试方法:绞丝经120℃干热处理8 min后测试负荷—伸长曲线;负荷—伸长曲线上以0.010 c N/dtex应力下的横坐标作为弹力起始点,以平行于断裂点与起始点连线的直线与拉伸曲线的切点作为弹力终点,计算弹性伸长率所需的绞丝弹性伸长量为起始点与终结点之间的伸长,绞丝原长为起始点对应的绞丝长度,测试绞数为10绞。
文摘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.
