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来自鸡砂囊的α-辅肌动蛋白:在低温下,肌动蛋白凝胶化活性的起始与肌动蛋白成束相关。

alpha-Actinin from chicken gizzard: at low temperature, the onset of actin-gelling activity correlates with actin bundling.

作者信息

Grazi E, Trombetta G, Magri E, Cuneo P, Schwienbacher C

机构信息

Instituto di Chimica Biologica, Università di Ferrara, Italy.

出版信息

Biochem J. 1994 Feb 15;298 ( Pt 1)(Pt 1):129-33. doi: 10.1042/bj2980129.

Abstract

The effect of alpha-actinin from chicken gizzard on the properties of F-actin solutions at 37 degrees C and at 4 degrees C was investigated. Beside the well-known increase of the gelling activity of alpha-actinin, it was found that lowering temperature to 4 degrees C: (a) modifies the shape of the alpha-actinin-F-actin binding isotherm; (b) increases the light scattering of the alpha-actinin-F-actin mixtures; (c) induces the formation of ribbons and bundles of F-actin. It was also observed that, by warming to 37 degrees C, the bundles of F-actin formed at 4 degrees C were dissociated into quasi-parallel actin filaments running at a distance of 25-42 nm from each other. On subsequent cooling to 4 degrees C, these parallel filaments were rapidly assembled into bundles. As at 37 degrees C, alpha-actinin displays a potent gelling activity on bundles but not on filaments of actin, and as the gelling activity at 4 degrees C is accompanied by the formation of actin bundles, it is concluded that actin bundling is a necessary condition to promote the actin-gelling activity.

摘要

研究了来自鸡胗的α-辅肌动蛋白在37℃和4℃下对F-肌动蛋白溶液性质的影响。除了众所周知的α-辅肌动蛋白凝胶活性增加外,还发现将温度降至4℃时:(a)改变了α-辅肌动蛋白-F-肌动蛋白结合等温线的形状;(b)增加了α-辅肌动蛋白-F-肌动蛋白混合物的光散射;(c)诱导形成F-肌动蛋白带和束。还观察到,升温至37℃时,在4℃形成的F-肌动蛋白束解离成彼此相距25-42nm的准平行肌动蛋白丝。随后冷却至4℃时,这些平行丝迅速组装成束。与在37℃时一样,α-辅肌动蛋白对肌动蛋白束而非肌动蛋白丝具有强大的凝胶活性,并且由于4℃时的凝胶活性伴随着肌动蛋白束的形成,得出结论:肌动蛋白成束是促进肌动蛋白凝胶活性的必要条件。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f208/1137992/8d1a66269e28/biochemj00093-0127-a.jpg

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