邻苯二甲醛对糖基化3－磷酸甘油醛脱氢酶的修饰及荧光性质的研究  

STUDY ON o- PHTHALADEHYDE MODIFICATION OF GLYCATED AND NONGLYCATED D-GLYCERALDEHYDE -3-PHOSPHATE DEHYDROGENASE

作　　者：赫荣乔[1] 

机构地区：[1]中国科学院生物物理研究所生物大分子国家重点实验室

出　　处：《生物物理学报》1994年第4期519-524,共6页Acta Biophysica Sinica

基　　金：生物物理所所长基金

摘　　要：ＯＰＴ修饰ＧＡＰＤＨ及ｇＧＡＰＤＨ的荧光衍生物与Ｔｒｐ残基之间存在非辐射的能量传递。在不同浓度的ＧｕＨＣｌ溶液中，糖基化和非糖基化酶ＯＰＴ衍生物的荧光的变化具有一定的差异。特别是两者的荧先在碘化钾溶液中的淬灭有明显的不同。ＯＰＴ修饰动力学研究表明，ｇＧＡＰＤＨ的修饰速度快于ＧＡＰＤＨ的修饰速度。以上结果提示：糖基化的位点可能在赖氨酸残基上，并且被糖基化的残基可能位于或靠近活性部位。It was demonstrated that the non-irradiation energy transfer from Trp residues to the OPT modified derivatives may occur for both GAPDH and gGAPDH. Changes in fluorescence emission of OPT modified derivatives for the both enzymes were different in GuHCl solutions of different concentrations, Especially, fluorescence quench of the derivatives of the both enzymes in KI solutions were markedly different . Kinetic modification of the enzymes showed that the rate of OPT modification of gGAPDH is appreciable faster than that of GAPDH. It appears that the glycated sites may be in situ at or near the active site of the molecule.

关 键 词：糖基化蛋白 邻二苯甲醛 荧光 磷酸甘油醛 脱氢酸 

分 类 号：Q71[生物学—分子生物学] Q510.1