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