%0 Journal Article
%T PURIFICATION AND PROPERTIES OF GLYCOLATE OXIDASE ISOZYME GO I FROM SPINACH LEAVES<br>菠菜乙醇酸氧化酶同工酶GO Ⅰ的纯化和特性
%A XU Jie
%A WU Yan-yan
%A <br>徐杰
%A 吴燕燕
%J 热带亚热带植物学报
%D 2001
%I 
%X By using ammonium sulfate fractionation, Sephadex G-25, DEAE-Cellulose, and Sepharose-6B chromatographies, glycolate oxidase isozyme GO Ⅰ was purified from spinach green leaves which showed only one band with molecular weight (Mr) of 40 000 + 2 000 in SDS-PAGE. The specific activity of purified GO Ⅰ was 8.4 U min-1mg-1 protein. GO Ⅰshowed its Mr of 470 000 in 4%-20% ND-PAGE and could catalyze both oxidations of glycolate and glyoxylate simultaneously. The isoelectric point (PI) of GO Ⅰ was about pH 7.4. There was a immunity precipitate line determined by immunity double-diffusion reaction between the antibody raised against GO Ⅰ and crude protein from spinach green leaves. The specific GO Ⅰ antibody was purified by protein A-Sepharose CL-4B column and specific antigen affinity elution. Only the 40 000 + 2 000 band could immunity cross-react with GO Ⅰ antibody, and different GO Ⅰ polymers of 470 000, 280 000, and 80 000 were found when crude protein were conduced to SDS-PAGE Western blot or ND-PAGE Western blot using this specific GO Ⅰ antibody.
%K Glycolate oxidase isozyme
%K Spinach
%K Catalyzed property
%K Isoelectric point
%K Molecular weight
%K Polymeric form<br>乙醇酸氧化酶同工酶
%K 菠菜
%K 催化特性
%K 等电点
%K 分子量
%K 聚合态
%K 纯化
%K 植物
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A74F042DF90151A4E3EF193E13FD5E1E&aid=82516464E2360B31&yid=14E7EF987E4155E6&vid=9CF7A0430CBB2DFD&iid=CA4FD0336C81A37A&sid=F3583C8E78166B9E&eid=13553B2D12F347E8&journal_id=1005-3395&journal_name=热带亚热带植物学报&referenced_num=1&reference_num=20