Chappell T G, Welch W J, Schlossman D M, Palter K B, Schlesinger M J, Rothman J E
Cell. 1986 Apr 11;45(1):3-13. doi: 10.1016/0092-8674(86)90532-5.
The synthetic peptide, VGIDLGTTYSC, derived from the heat shock-induced genes human hsp70, Drosophila hsp70, S. cerevisiae YG100, and E. coli dnaK, elicited antibodies that recognized two constitutive proteins in bovine extracts. One of these proteins, 71 kd, has previously been identified as uncoating ATPase, an enzyme that releases clathrin from coated vesicles. This immunological data complemented the result that uncoating ATPase was indistinguishable from the constitutive mammalian 71 kd stress protein by either partial proteolytic mapping or two-dimensional gel analysis. In addition, affinity-purified uncoating ATPase antibodies recognize proteins in yeast identified as the gene products of the heat shock or heat shock cognate genes YG100 and YG102. The results show that uncoating ATPase is a member of the 70 kd heat shock protein family.
源自热休克诱导基因人类hsp70、果蝇hsp70、酿酒酵母YG100和大肠杆菌dnaK的合成肽VGIDLGTTYSC，能引发识别牛提取物中两种组成型蛋白的抗体。其中一种蛋白，71kd，先前已被鉴定为脱衣ATP酶，一种从被膜小泡释放网格蛋白的酶。这一免疫学数据补充了以下结果：通过部分蛋白水解图谱或二维凝胶分析，脱衣ATP酶与组成型哺乳动物71kd应激蛋白无法区分。此外，亲和纯化的脱衣ATP酶抗体识别酵母中被鉴定为热休克或热休克同源基因YG100和YG102基因产物的蛋白。结果表明，脱衣ATP酶是70kd热休克蛋白家族的一员。
