%0 Journal Article
%T DETERMINATION OF THE SUGAR BOUND TO D-GLYCERADEHYDE-3-PHOSPHATE DEHYDROGENASE AND STUDY ON CONFORMATIONAL CHANGES OF THE ENZYME<br>糖基化3－磷酸甘油醛脱氢酶的含糖量及其构象变化
%A 赫荣乔
%J 生物物理学报
%D 1994
%I 
%X The determination of the sugar bound to GAPDH and investigation of conformational changes of the glycatal and non-glycated GAPDH have been performed by methods of orcinol sulfuric acid, phenol sulfuric acid, CD, fluorescence and DTNB modifying.The glycatal GADPH which purified by the affinity chromatography of m-aminophenylboronic acid linked to Sepharose CL 6B should consist of 1.89 glucose.The cirvular dichroism spectra between gGAPDH and GPADH were appreciable different in the near ultraviolet region, but less in the far ultraviolet region. That changes in intrinsic fluoresence between the two.enzyme are distinct in GuHCl solutions of different concentrations were also observed. The kinetic of modification of the nonglycated enzyme was a biphasic proedure which can be divided into fast and slow phase. But that of the gGAPDH is a triphasic one which may be divided into fast, luteinte and slow phase. The fast phase of gGAPDH is faster than that of GAPDH during DTNB modification. It is suggestal that glycation of enzyme might lead to some changes in conformation of the active site and the molecule as a whole,the glycation might occur at Lys residues which may be in situ at or near the active site.
%K D-glyceraldehyde-3-phosphate
%K dehydrogenase
%K Glycation Glycated protein
%K Fluorescence
%K CD Conformation<br>糖基化
%K 磷酸甘油酸
%K 构象
%K 荧光
%K 脱氢酶
%K 含糖量
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=7C6DDDFF97F6AD15848F5C325996942B&yid=3EBE383EEA0A6494&vid=F3090AE9B60B7ED1&iid=38B194292C032A66&sid=3E3EF0DB5E6F2DA9&eid=2E41258BCB9A7DB2&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=2&reference_num=4