Matsuo M, Hamato N, Takano R, Kamei-Hayashi K, Yasuda-Kamatani Y, Nomoto K, Hara S
Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology, Japan.
Biochim Biophys Acta. 1992 Apr 8;1120(2):187-92. doi: 10.1016/0167-4838(92)90268-i.
Two almost identical trypsin isoinhibitors, LLDTI-I and LLDTI-II, from bottle gourd (Lagenaria leucantha Rusby var. Depressa Makino) seeds were purified by acetone precipitation, gel filtration and reversed phase chromatography. LLDTI-I and LLDTI-II consist of 30 and 29 amino acid residues, respectively, and have identical sequences, except that LLDTI-I has one additional pyroglutamic acid residue at N-terminus. Both proteins are strong inhibitors of bovine trypsin, with Ki values of 2.4.10(-10) M (LLDTI-I) and 9.6.10(-11) M (LLDTI-II). Amino acid sequences are as follows: [sequence: see text]
从瓠瓜（Lagenaria leucantha Rusby var. Depressa Makino）种子中纯化出两种几乎相同的胰蛋白酶抑制因子LLDTI-I和LLDTI-II，采用了丙酮沉淀、凝胶过滤和反相色谱法。LLDTI-I和LLDTI-II分别由30和29个氨基酸残基组成，除LLDTI-I在N端多一个焦谷氨酸残基外，二者序列相同。两种蛋白质都是牛胰蛋白酶的强效抑制剂，LLDTI-I的Ki值为2.4×10⁻¹⁰ M，LLDTI-II的Ki值为9.6×10⁻¹¹ M。氨基酸序列如下：[序列：见原文]
