作者: Shigeo Kubota , H.W. Yeung , Jen Tsi Yang
DOI: 10.1016/0167-4838(86)90138-X
关键词:
摘要: The conformations of three abortifacient proteins, trichosanthin from the Chinese herb Tianhuafen and alpha- beta-momorcharin Kuguazi, were studied by circular dichroism. Their spectra in ultraviolet region (188-250 nm) similar to each other also pH-independent (between pH 5 9). All proteins contained about 30% helix, as compared with 39% for X-ray diffraction study, 40-60% beta-sheets, but had no beta-turns, suggesting a structural homology among proteins. addition 20 mM sodium dodecyl sulfate nearly doubled helicity at expense beta-sheets small effect on conformation alpha-momorcharin, whereas corresponding change was between two momorcharins. This implies marked difference stability against surfactant.