PURIFICATION AND STRUCTURAL-ANALYSIS OF MYOSINS FROM BRAIN AND OTHER NON-MUSCLE TISSUES

PURIFICATION AND STRUCTURAL-ANALYSIS OF MYOSINS FROM BRAIN AND OTHER NON-MUSCLE TISSUES
复制标题

DOI:
10.1016/s0022-2836(75)80154-9
复制
发表时间:
1975-01-01
影响因子:
5.6
通讯作者:
BRAY, D
BRAY, D
中科院分区:
生物学2区
文献类型:
--
作者:
BURRIDGE, K;BRAY, D

文献摘要

被引文献

相似文献

开发了一种从鸡胚胎的大脑中纯化肌球蛋白的方法,并应用于鸡的其他组织,包括肌肉和非肌肉组织。脑蛋白被发现与肌球蛋白总体上相似,但并不完全相同。它在大小和亚基组成上与砂囊(平滑肌)肌凝蛋白非常接近,在atp酶活性和与肌动蛋白的相互作用上与肌凝蛋白相似。然而,它在透析低离子强度缓冲液时形成了一种独特的大的副晶阵列,并在半胱氨酸残基的部分蛋白质水解或化学裂解上形成了独特的肽模式。来自砂囊、脑、输卵管、肾脏、血小板以及培养的成纤维细胞、肝细胞和交感神经元的肌球蛋白,在十二烷基硫酸钠存在的情况下,在丙烯酰胺凝胶中进行电泳时表现相似,特别是显示出两种分子量接近20,000和17,000的成分。化学裂解法分析肌球蛋白重链,发现胸肌(骨骼肌)、心肌(心肌)、砂囊(平滑肌)、血小板和脑肌球蛋白在结构上存在较大差异。其他组织的肌凝蛋白似乎由两种或两种以上的肌凝蛋白混合而成。提示细胞质肌球蛋白至少存在两种重链不同、轻链相近的细胞质肌球蛋白,并可能在某些细胞中共存。
A procedure was developed for the purification of myosin from the brains of chick embryos and applied to other chicken tissues, both muscle and non-muscle. The brain protein was found to have an overall similarity to muscle myosins but not to be identical. It was very close in size and subunit composition to gizzard (smooth muscle) myosin, and was myosin-like in its ATPase activity and interaction with actin. However, it formed large paracrystalline arrays of a unique kind on dialysis against buffers of low ionic strength, and gave a distinctive pattern of peptides on partial proteolysis or chemical cleavage at cysteine residues.Myosins from gizzard, brain, oviduct, kidney, blood platelets, and cultures of fibroblasts, liver cells and sympathetic neurones, all behaved similarly on electrophoresis in acrylamide gels in the presence of sodium dodecyl sulphate and, in particular, revealed two components with molecular weights close to 20,000 and 17,000. Analysis of myosin heavy chains by chemical cleavage showed major differences in structure between breast (skeletal muscle), cardiac (heart muscle), gizzard (smooth muscle), platelet and brain myosins. The myosins of other tissues appeared to comprise a mixture of two or more of these types.It is suggested that at least two kinds of cytoplasmic myosin exist which have different heavy chains but closely similar light chains, and that both types might coexist in some cells.