使用改进方法制备的重酶解肌球蛋白对肌动蛋白丝双向聚合偏向性的证据。
Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method.
作者信息
Woodrum D T, Rich S A, Pollard T D
出版信息
J Cell Biol. 1975 Oct;67(1):231-7. doi: 10.1083/jcb.67.1.231.
Abstract
Isolated actin filaments decorated with HMM can grow by addition of actin monomers to either end, although there is a bias toward addition at the end which is normally attached to the Z line in striated muscle.
摘要
用重酶解肌球蛋白修饰的分离肌动蛋白丝，可通过在任一端添加肌动蛋白单体而生长，尽管在通常与横纹肌中Z线相连的那一端添加有偏向性。
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本文引用的文献
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The cooperative nature of G-F transformation of actin.肌动蛋白G-F转换的协同性质
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Formation of arrowhead complexes with heavy meromyosin in a variety of cell types.在多种细胞类型中与重酶解肌球蛋白形成箭头状复合物。
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The polymerization of actin: its role in the generation of the acrosomal process of certain echinoderm sperm.肌动蛋白的聚合作用：其在某些棘皮动物精子顶体突起形成过程中的作用。
J Cell Biol. 1973 Oct;59(1):109-26. doi: 10.1083/jcb.59.1.109.
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Actin and myosin and cell movement.肌动蛋白、肌球蛋白与细胞运动。
CRC Crit Rev Biochem. 1974 Jan;2(1):1-65. doi: 10.3109/10409237409105443.
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