Lee-Eiford A, Ow R A, Gibbons I R
J Biol Chem. 1986 Feb 15;261(5):2337-42.
Irradiation of soluble dynein 1 from sea urchin sperm flagella at 254 nm in the presence of 50 microM ATP and 100 microM inorganic vanadate (Vi) cleaves the alpha and beta heavy chains into approximately equal quantities of two polypeptides of Mr 228,000 and 200,000, with a conversion efficiency of about 63%. A similar cleavage occurs in the presence of Vi and either ADP or 8-azidoadenosine 5'-triphosphate (8-N3ATP); in the latter case, 8-N3ATP becomes covalently bound principally to the Mr 228,000 polypeptide. No detectable amount of these fragments is formed if either the Vi or the nucleotide is omitted or in the presence of Vi and 50 microM AMP. These results emphasize the basic similarity of the two ATPases associated with the alpha and beta heavy chain subunits of dynein 1 and give a mean Mr of 428,000 for the intact heavy chains.
在存在50微摩尔ATP和100微摩尔无机钒酸盐（Vi）的情况下，用254纳米波长的光照射海胆精子鞭毛中的可溶性动力蛋白1，可将α和β重链切割成分子量约为228,000和200,000的两种多肽，且数量大致相等，转化效率约为63%。在存在Vi以及ADP或8-叠氮腺苷5'-三磷酸（8-N3ATP）的情况下也会发生类似的切割；在后一种情况下，8-N3ATP主要与分子量为228,000的多肽共价结合。如果省略Vi或核苷酸，或者在存在Vi和50微摩尔AMP的情况下，则不会形成可检测到的这些片段。这些结果强调了与动力蛋白1的α和β重链亚基相关的两种ATP酶的基本相似性，并得出完整重链的平均分子量为428,000。
