Welch W J
J Biol Chem. 1985 Mar 10;260(5):3058-62.
Rat embryo fibroblast cells grown under stress (e.g. heat shock, arsenite, or amino acid analogue treatment) show elevated levels of a number of proteins with apparent molecular masses between 28,000-110,000 daltons (i.e. stress proteins). It is shown that the smaller 28,000-dalton stress proteins, which do not contain methionine, are comprised of at least four isoforms, all of which appear related as determined by one-dimensional peptide mapping. [32P]H3PO4 labeling of normal and stressed cells demonstrates that three of the four 28-kDa isoforms are phosphoproteins. In the course of other studies phosphorylation of two 28,000-dalton proteins was observed in quiescent rat embryo fibroblasts following the addition of either the phorbol diester, phorbol-12-myristate-13 acetate, a calcium ionophore, A23187, or simply fresh serum. It is shown here that these two 28,000-dalton proteins are in fact two of the 28 kDa mammalian stress proteins.
在应激条件下（如热休克、亚砷酸盐或氨基酸类似物处理）培养的大鼠胚胎成纤维细胞中，若干表观分子量在28,000至110,000道尔顿之间的蛋白质（即应激蛋白）水平升高。结果表明，不含甲硫氨酸的较小的28,000道尔顿应激蛋白至少由四种同工型组成，通过一维肽图谱分析确定，所有这些同工型似乎都有关系。正常细胞和应激细胞的[32P]H3PO4标记表明，四种28 kDa同工型中的三种是磷蛋白。在其他研究过程中，在静止的大鼠胚胎成纤维细胞中加入佛波酯、佛波醇-12-肉豆蔻酸酯-13-乙酸酯、钙离子载体A23187或仅仅新鲜血清后，观察到两种28,000道尔顿蛋白质的磷酸化。本文表明，这两种28,000道尔顿的蛋白质实际上是28 kDa哺乳动物应激蛋白中的两种。
