%0 Journal Article
%T STUDIES ON THE PURIFICATION AND PROPERTIES OF OMPHALIA LAPIDESCENS LECTIN<br>雷丸凝集素的纯化及理化性质的研究
%A YU Yong-Hai
%A GONG Jun
%A YU Ming-Kun
%A <br>于勇海
%A 龚隽
%A 余明琨
%J 菌物学报
%D 2000
%I 
%X Omphalia lapideacens lectin (OLL) has been purified by extraction with Tris-HCl buffer,anunonium sulfate frachonation, ion-exchange column, and affinity chromatograPhy on an ovomucoid-Sepharose 4B column and Sephacryl-S100 column. The purified OLL shows an achvity increase of 45.8 fold, an achvity recovery of 2.5% and purity of above 95%. The hemagglutinating activity of OLL on rabbit red blood cel1s was inhibited by D-galactose. The molecular weight of OLL was 12kD OLL was heat stable and it was comparahvely stable at pH values from 1 to 12. Zinc Chioride (2mmol / L) incfeasedit,s hemapgluhnating achvity by 4 fold and the hemagglutinahng activity of OLL on human red blood cells was increased by 4 fold. Cireular dichroism spectra revealed high content of a-helix and -sheet structures in this lectin. From the spectrum observed in the presence of D-galactose, the structure of OLL has some change and become more tight.
%K Lectin
%K OLL
%K Omphalia lapideacens
%K physical and chamical properties<br>凝集素
%K 雷丸凝集素
%K 雷丸
%K 理化性质
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=CA9F815FCB0F62294C4266BB6F902ACB&aid=0398338BD7FF02C3&yid=9806D0D4EAA9BED3&vid=2A8D03AD8076A2E3&iid=0B39A22176CE99FB&sid=B4E8EA49DAAEB84F&eid=4133DDB79B497495&journal_id=1672-6472&journal_name=菌物学报&referenced_num=0&reference_num=7