Someya A, Nagaoka I, Yamashita T
Department of Biochemistry, Juntendo University, School of Medicine, Tokyo, Japan.
FEBS Lett. 1993 Sep 13;330(2):215-8. doi: 10.1016/0014-5793(93)80276-z.
A 260 kDa cytosolic complex (SP-1) was purified from guinea pig neutrophils. SP-1 was composed of 63 kDa, 47 kDa and 39 kDa proteins. The 63 kDa and 47 kDa proteins proved to correspond to human p67phox and p47phox by Western blot analysis, whereas Western blot and amino acid sequence analyses revealed that the 39 kDa protein was a novel protein. The 47 kDa protein was separated from the 63 kDa and 39 kDa proteins by dithiothreitol (DTT)-treatment. On the other hand, the 63 kDa and 39 kDa proteins were not separated with DTT, detergent and ethanol treatment. These results suggest that the 39 kDa protein tightly associates with the 63 kDa protein and may regulate the function of the 63 kDa protein.
从豚鼠中性粒细胞中纯化出一种260 kDa的胞质复合物（SP-1）。SP-1由63 kDa、47 kDa和39 kDa的蛋白质组成。通过蛋白质免疫印迹分析证明，63 kDa和47 kDa的蛋白质分别对应于人p67phox和p47phox，而蛋白质免疫印迹和氨基酸序列分析表明，39 kDa的蛋白质是一种新蛋白。通过二硫苏糖醇（DTT）处理，47 kDa的蛋白质与63 kDa和39 kDa的蛋白质分离。另一方面，DTT、去污剂和乙醇处理均未使63 kDa和39 kDa的蛋白质分离。这些结果表明，39 kDa的蛋白质与63 kDa的蛋白质紧密结合，并可能调节63 kDa蛋白质的功能。
