Structure-activity relationship of a hemagglutinin from Moringa oleifera seeds.
作者： Uma V. Katre , C.G. Suresh , M. Islam Khan , Sushama M. Gaikwad
DOI: 10.1016/J.IJBIOMAC.2007.10.024
关键词:
摘要: The hemagglutinin from the seeds of Moringa oleifera (MoL) agglutinates human as well rabbit erythrocytes; affinity for latter is almost 250 times more than that former. MoL was inhibited by glycoproteins namely thyroglobulin, fetuin and holotransferin indicating complex sugar specificity lectin. protein a homodimer with molecular mass 14kDa, subunits (7.1kDa) linked disulfide bond(s). secondary structure elements are alpha-helix, 28%; beta-sheet, 23%; turn 20% unordered 28%. While activity were not affected at extreme pH high temperature, they drastically in presence dithiothreitol above 7.0, linkages hold active conformation protein.
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