Svendsen I, Nicolova D, Goshev I, Genov N
Department of Chemistry, Carlsberg Laboratory, Copenhagen Valby, Denmark.
Int J Pept Protein Res. 1994 May;43(5):425-30. doi: 10.1111/j.1399-3011.1994.tb00540.x.
A protein with inhibitory activity toward trypsin has been isolated from Sinapis arvensis L (charlock). It has a molecular weight of 15,500 and consists of two chains connected by disulfide bonds. The amino acid sequence was determined and showed that it belongs to the napin family of storage proteins. CD studies showed an alpha-helix content of 12% and a beta-structure of about 50%.
从野芥菜(Sinapis arvensis L)中分离出了一种对胰蛋白酶具有抑制活性的蛋白质。它的分子量为15,500,由两条通过二硫键连接的链组成。测定了其氨基酸序列,结果表明它属于贮藏蛋白的napin家族。圆二色性研究显示其α-螺旋含量为12%,β-结构约为50%。