Effects of Denaturation and Amino Acid Modification on Fluorescence Spectrum and Hemagglutinating Activity of Hericium erinaceum Lectin

作     者：Meng GONG, Jie AN, Hong-Zhou Lü, Chuan-Fang WU, Yi-Jin LI, Jing-Qiu CHENG, and Jin-Ku BAO*College of Life Sciences, Sichuan University, Chengdu 610064, China Meng GONG, Jie AN, Hong-Zhou Lü, Chuan-Fang WU, Yi-Jin LI, Jing-Qiu CHENG, and Jin-Ku BAO*College of Life Sciences, Sichuan University, Chengdu 610064, China

作者机构：College of Life Sciences Sichuan University 

出 版 物：《Acta Biochimica et Biophysica Sinica》 (生物化学与生物物理学报(英文版))

年 卷 期：2004年第36卷第5期

页      面：343-350页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 

基　　金：This work was supported by a grant from the National Natural Science Foundation of China (General Program) (No. 30000032) 

主　　题：sialic acid-binding lectin Hericium erinaceum lectin fluorescence spectrum and fluores- cence quenching hemagglutinating activity chemical modification 

摘      要：A sialic acid-binding lectin (Hericium erinaceum lectin, HEL), isolated from fresh fruiting bodies of Hericium erinaceum, was treated with various temperature and pH to investigate its fluorescence spectra and hemagglutinating activity. It was found that the hemagglutinating activity of HEL was relatively steady below 60 °C and at pH from 6 to 11, and the change of hemagglutinating activity was relative to the change of hydrophobic areas where tryptophan residues located. In fluorescence quenching study of HEL by acrylamide and KI, it was indicated that nearly all the tryptophan residues of HEL located on the surface of the molecule, and most of them were in hydrophobic areas or negatively charged areas. Chemical modifica- tion of HEL proved that there were about twelve tryptophan residues in a HEL molecule and all of them were located on the surface or in the shallow groove of the molecule, and eight of them were essential for hemag- glutinating activity; aspartic acid or glutamic acid residues were involved in maintaining the crucial confor- mation of activity center and made great contribution to the hemagglutinating activity of HEL, but they could not touch the sialic acid molecule directly; tyrosine residues also played a role in the hemagglutinating activ- ity of HEL; while arginine, serine, threonine, histidine residues had no effect on the hemagglutinating activity of HEL.