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Effects of Denaturation and Amino Acid Modification on Fluorescence Spectrum and Hemagglutinating Activity of hericium erinaceum lectin

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Acta Biochimica et Biophysica Sinica 2004年第5期36卷 343-350页

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 College of Life Sciences Sichuan University Chengdu 610064 China

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.

关键词： sialic acid-binding lectin hericium erinaceum lectin fluorescence spectrum and fluores- cence quenching hemagglutinating activity chemical modification

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