%0 Journal Article
%T Expression and inhibitory activity analysis of a 25-kD Bowman-Birk protease inhibitor in rice
%A CHEN Jun
%A MAO Shengji
%A XIE Yang
%A CAO Zhongren
%A ZHANG Yan
%A LIU Jing
%A CHEN Zhangliang
%A QU Lijia
%A GU Hongya
%A <br>CHEN
%A Jun
%A MAO
%A Shengji
%A XlE
%A Yang
%A CAO
%A Zhongren
%A ZHANG
%A Yan
%A LIU
%A jing
%A CHEN
%A Zhangliang
%A QU
%A Lijia
%A GU
%A Hongya
%J 科学通报(英文版)
%D 2006
%I 
%X Rice Bowman-Birk inhibitors (RBBI), with one (8 kD) or two homologous domains (16 kD), were found to be effective trypsin inhibitors in vitro. In this study, we demonstrate that the 25-kD protein corresponding to the three-domain RBBI indeed ex- ists in rice in planta, and that the RBBIs are regulated by development and wounding. We also found by inhibitory activity assay that the 3:13 disulfide bond, but not the 4:5 disulfide bond, suppresses the tryp- sin-inhibitory activity, and the D3 domain of RBBI3-1 has no inhibitory activity against trypsin, chymotryp- sin, paparin or subtilisin. Mutation analyses showed that conversion from Lys to Leu or Tyr in the N-terminal P1 site in D1 domain did not create chy- motrypsin-inhibitory activity, suggesting that the structure of the reactive loop in D1 domain hinder the new inhibitory specificity at P1 site, and the chy- motrypsin-inhibitory activity might need the participa- tion of other structures, e.g. 3:13 disulfide bond.
%K Bowman-Birk inhibitor
%K trypsin-inhibitory activity
%K chy- motrypsin-inhibitory activity
%K disulfide bond<br>水稻
%K RBBI
%K 双硫键
%K 胰凝乳蛋白酶
%K 胰岛素
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=01BA20E8BA813E1908F3698710BBFEFEE816345F465FEBA5&cid=96E6E851B5104576C2DD9FC1FBCB69EF&jid=DD6615BC9D2CFCE0B6F945E8D5314523&aid=E362A7A9290E7DB11BCD16EA1266E1DA&yid=37904DC365DD7266&vid=987EDA49D8A7A635&iid=CA4FD0336C81A37A&sid=318E4CC20AED4940&eid=95D537AC89B28832&journal_id=1001-6538&journal_name=科学通报(英文版)&referenced_num=0&reference_num=28