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机构地区:[1]中国科学院生物物理研究所
出 处:《生物物理学报》1995年第1期16-20,共5页Acta Biophysica Sinica
摘 要:对α-mmc及β-mmc进行了溶剂微扰差光谱的研究及在不同温度条件下的光谱滴定,结合最新得到的α-mmc的晶体结构进行了分析和讨论,并与天花粉蛋白的紫外光谱进行了比较。The environment of tyrosine residues in α-momocharin (α-mmc) and β-momocharin (β-mmc) has been investigated by solvent perturbation differencr spectroscopy. Serveral perturbants with different molecular dimensions were used in pH range of 8.6 to 2.5. The results show that approximately 40%-50% of the twelve phenolic groups are 'exposed' and the rest are 'buried' in the interior of α-mmc and β-mmc. The effect of the various perturbants with different molecular dimensions at each pH value, except for D2O at pH8.6 are almost the same.Spectrophotometric titration has been carried out at 25℃, 40℃ for α-mmc, and 25℃, 35℃ for β-mmc. The titration curves of this two proteins have been shown to be of three steps. The first step take place at pH below 11.5,it is reversibe; The second step around pH 11.5- 12.0 at 25℃ and 11.0-11.5 at 40℃ for α-mmc and 35℃ for β-mmc,respectively. At pH above 12, the titration curve has a third step, suggesting that this two protein molecules have a rether stable core.Discussion has been made in relation to the crystal structure of a-mmc and the ultraviolet spectrocopy of TCS studied by our group recently.
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