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钙调蛋白结合蛋白,一种与钙调蛋白结合、与F肌动蛋白相互作用的蛋白质,存在于主动脉、子宫和血小板中。

Caldesmon, a calmodulin-binding, F actin-interacting protein, is present in aorta, uterus and platelets.

作者信息

Kakiuchi R, Inui M, Morimoto K, Kanda K, Sobue K, Kakiuchi S

出版信息

FEBS Lett. 1983 Apr 18;154(2):351-6. doi: 10.1016/0014-5793(83)80181-1.

Abstract

Caldesmon, a protein originally found in chicken gizzard, was concluded also to be present in bovine aorta, uterus, and human platelets by demonstration of a protein with the following properties: (a) Ca2+-dependent calmodulin-binding; (b) binding to F actin in such way that the binding was broken on Ca2+-dependent binding of calmodulin; (c) cross-reactivity in immune blotting procedures with affinity-purified antibody against gizzard caldesmon; (d) similar subunit Mr-values on SDS-gel to those of gizzard caldesmon. Like gizzard caldesmon, platelet caldesmon was composed of two polypeptide bands of Mr 150 000 and 147 000, but caldesmon in aorta and uterus gave a single band of Mr 150 000. A polypeptide of Mr 165 000 that was immunologically distinct from caldesmon but, like caldesmon, bound to calmodulin and F actin in a flip-flop fashion, was also demonstrated in aorta and uterus.

摘要

钙调蛋白最初是在鸡胗中发现的一种蛋白质,通过对具有以下特性的蛋白质进行鉴定,得出它也存在于牛主动脉、子宫和人血小板中:(a)依赖Ca2+的钙调蛋白结合;(b)以这样一种方式与F肌动蛋白结合,即这种结合在钙调蛋白依赖Ca2+的结合时被破坏;(c)在免疫印迹程序中与抗鸡胗钙调蛋白的亲和纯化抗体发生交叉反应;(d)在SDS凝胶上的亚基Mr值与鸡胗钙调蛋白的相似。与鸡胗钙调蛋白一样,血小板钙调蛋白由Mr为150 000和147 000的两条多肽带组成,但主动脉和子宫中的钙调蛋白给出一条Mr为150 000的带。在主动脉和子宫中还证实了一种Mr为165 000的多肽,它在免疫上与钙调蛋白不同,但与钙调蛋白一样,以翻转方式与钙调蛋白和F肌动蛋白结合。

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