Hirata T, Izumi S, Tsuji S
Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Japan.
Biosci Biotechnol Biochem. 1999 Oct;63(10):1816-8. doi: 10.1271/bbb.63.1816.
A 20-kDa protein (p20) with a GTP binding activity was purified from the cultured cells of Glycine max (soybean). The amino acid sequence of p20 showed 65% identity in a 23 amino acid overlap against the Kunitz-type trypsin inhibitor of soybean reported. Furthermore, it was found that a Kunitz-type soybean trypsin inhibitor of commercial origin also binds GTP.
从大豆(Glycine max)培养细胞中纯化出一种具有GTP结合活性的20 kDa蛋白质(p20)。p20的氨基酸序列在23个氨基酸重叠区域与已报道的大豆Kunitz型胰蛋白酶抑制剂有65%的同一性。此外,还发现市售来源的Kunitz型大豆胰蛋白酶抑制剂也能结合GTP。