STUDIES ON THE PURIFICATION AND PROPERTIES OF OMPHALIA LAPIDESCENS LECTIN
雷丸凝集素的纯化及理化性质的研究

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.