%0 Journal Article
%T A STUDY ON THE FOLDING OF CREATINE KINASES FROM HUMAN AND RABBIT MUSCLE AT LOW pH<br>人肌和兔肌肌酸激酶在低pH条件下再折叠的研究
%A Li Jinping
%A Hob Lixiang
%A Zhou Haimeng
%A <br>李锦平
%A 侯立向
%A 周海梦
%J 生物物理学报
%D 1994
%I 
%X The confonnational stabal of cleatjne the from human and rabbit muscle at acidic pHun examined by the intrinsic proch fluoascence and far--ultlaviolet cellular dichIDism(far--UV CD). The adults we obtained show that at low iohic singtin, by adding HCl, tonative ha and rabbit creatine kinals ash proteins tended to adopt almost an fillly tmfolded confonnational state in the vicely of PH 2.0. Their tryptophan fluorescenceemission had a lhawh at the indicating a complete exposure of the nyptophan asiduesto the solvent. Thed far--UV CD spectla shoal partly disonled secondary str uperthg, butthe se dena Proteins retained soak secondary strucks. However, at high ionic strength andlow PH an in inte confonnational state (molten-globule state) which was fnSt discoverby Goto et al un also olived in our pat experiment . This intointe had a secondary thestructute similar to that of the nahve enzyme. The tryptophan fluorescence spectla were similar,with a mhanum at 335nm to that of the native on, indicating that the protein is almostrefolded complmp. Hoal, the intenSity of fluorescence elnjssion was much lower than thato f native enzyme, indicating that this state is more mobile and adulting in dynamicfluo quenching. The present adults support Goto's discovery. It is suggeStal thatmolten-globule state opt be an nounal folding lute-iate state of proteins.
%K Crmtine kinase Acid-denaturation Unfolding and refolding Molten -globule state<br>肌酸激酶
%K 酸变性
%K 去折叠与再折叠
%K 融球中间体
%K 蛋白质折叠
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=7C6DDDFF97F6AD15E95C516649831D40&yid=3EBE383EEA0A6494&vid=F3090AE9B60B7ED1&iid=CA4FD0336C81A37A&sid=6209D9E8050195F5&eid=2001E0D53B7B80EC&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=2&reference_num=2