%0 Journal Article
%T BjCHI1 from Brassica juncea Displays both Chitinase and Agglutination Activity<br>兼具凝集素活性的芥菜几丁质酶BjCHI1
%A CHYE Mee-Len
%A RAM Sathishkvmar
%A <br>欧阳石文
%A 赵开军
%A 冯兰香
%A CHYE
%A Mee-Len
%A RAM
%A Sathishkvmar
%J 生物工程学报
%D 2002
%I 
%X The proteins encoded by the Brassica juncea chitinase gene BjCHI1 and its derived genes BjCHI2 and BjCHI3 were expressed by Multi-copy Pichia expression system. The chitinase activity of FPLC purified BjCHI1, BjCHI2 and BjCHI3 were tested and the results showed that all the three proteins degraded both CM-chitin-RBV and colloidal chitin. The Km values of BjCHI1, BjCHI2 and BjCHI3 for CM-chitin-RBV were estimated as 0.799 mg/mL, 0.544 mg/mL and 0.793 mg/mL, respectively. When the colloidal chitin was used as substrate, the Km values were 0.281 mg/mL, 0.388 mg/mL and 1.643 mg/mL, respectively, indicating chitin-binding domain can increase affinity of chitinase to insoluble substrate. In the agglutination activity assay, only BjCHI1 shows activity when the protein concentration was more than 33 micrograms/mL, while BjCHI2 and BjCHI3 without agglutination activity even when the concentration was increased as high as 800 micrograms/mL. This means that the two chitin-binding domains in BjCHI1 are essential for agglutination and BjCHI1 is the first protein which shows both chitinase and agglutination activity identified so far in plants.
%K BjCHI1
%K chitinase
%K agglutination
%K Km<br>BjCHI1，几丁质酶，
%K 凝集素，
%K Km
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=6669E4EFF6822C0E&yid=C3ACC247184A22C1&vid=13553B2D12F347E8&iid=94C357A881DFC066&sid=6A9657F54F754BF6&eid=52B9DFFFCC2EB041&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=16