小鼠肥大细胞瘤细胞中69,000道尔顿和68,000道尔顿热休克蛋白可能的细胞骨架关联以及热休克蛋白之间的结构关系。
Possible cytoskeletal association of 69,000- and 68,000-dalton heat shock proteins and structural relations among heat shock proteins in murine mastocytoma cells.
作者信息
Ohtsuka K, Tanabe K, Nakamura H, Sato C
出版信息
Radiat Res. 1986 Oct;108(1):34-42.
When murine mastocytoma cells (FMA 1) were heat shocked (42 degrees C for 4 h), nine heat shock proteins (HSPs) were detected by two-dimensional gel electrophoresis. Their apparent molecular weights were 100, 85, 69, 68, 32, 30, and 23 kDa (3 of 23 kDa). The structural homology of 4, 69, 68, 32, and 30 kDa, was demonstrated by two-dimensional tryptic peptide mapping. The 69- and 68-kDa HSPs were purified and rabbit antisera against these HSPs were prepared. A small fraction (less than 10%) of the 69- and 68-kDa HSPs were copurified with the microtubules and were present in the Triton X-100/KCl cytoskeletal fraction as shown by immunoblotting with the antiserum and by peptide mapping. Our results are consistent with the hypothesis of a cytoskeletal role for HSPs.
当鼠肥大细胞瘤细胞（FMA 1）受热休克（42摄氏度，持续4小时）时，通过二维凝胶电泳检测到9种热休克蛋白（HSPs）。它们的表观分子量分别为100、85、69、68、32、30和23 kDa（23 kDa的有3种）。通过二维胰蛋白酶肽图谱分析证明了4、69、68、32和30 kDa的结构同源性。纯化了69 kDa和68 kDa的热休克蛋白，并制备了针对这些热休克蛋白的兔抗血清。如用抗血清进行免疫印迹和肽图谱分析所示，69 kDa和68 kDa热休克蛋白的一小部分（小于10%）与微管共纯化，并存在于Triton X-100/KCl细胞骨架组分中。我们的结果与热休克蛋白具有细胞骨架作用的假说一致。
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