N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions.
N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions.
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N-乙基胺化的重霉素。肌动球蛋白相互作用的探针。
DOI：
10.1083/jcb.82.1.57
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发表时间：
1979-07
影响因子：
7.8
通讯作者：
Cande, W Z
中科院分区：
文献类型：
--
作者：
Meeusen, R L;Cande, W Z
用巯基试剂N-乙基马来酰亚胺(NEM)处理兔骨骼肌重肌球蛋白(HMM)产生一种HMM，在有镁三磷酸腺苷存在的情况下，它仍然与肌动蛋白紧密结合。NEM-HMM与肌动蛋白形成特征的“箭头”复合体，即使用镁三磷酸腺苷漂洗，这种复合体仍然存在。NEM-HMM抑制肌动蛋白的激活、肌动球蛋白的超沉淀、甘油肌原纤维的收缩以及土壤杂乱卡罗林阿米巴细胞质链的收缩。然而，NEM-HMM不干扰去膜纤毛的体外微管聚合或搏动。
Treatment of rabbit skeletal muscle heavy meromyosin (HMM) with the sulfhydryl reagent N-ethylmaleimide (NEM) produces a species of HMM which remains tightly bound to actin in the presence of MgATP. NEM-HMM forms characteristic "arrowhead" complexes with actin which persist despite rinses with MgATP. NEM-HMM inhibits the actin activation of native HMM-ATPase activity, the superprecipitation of actomyosin, the contraction of glycerinated muscle myofibrils, and the contraction of cytoplasmic strands of the soil amoeba Chaos carolinensis. However, NEM- HMM does not interfere with in vitro microtubule polymerization or beating of demembranated cilia.