Different Thermostability of Skeletal Muscle Glyceraldehyde-3-phosphate Dehydrogenase from Hibernating and Euthermic Jerboa (Jaculus orientalis)

作     者：IDDAR Abdelghani,CAMPOS Luis A.,SANCHO Javier,SERRANO Aurelio,SOUKRI Abdelaziz 

作者机构：Laboratoire de Biochimie Departamento de Bioquímica y Biología Molecular y Celular Departamento de Bioquímica y Biología Molecular y Celular Instituto de Bioquímica Vegetal y Fotosíntesis Laboratoire de Biochimie Unitè de Gènie Enzymatique et Biologie Molèculaire Facultè des Sciences-Ain Chock Casablanca Morocco Universidad de Zaragoza Zaragoza Spain Universidad de Zaragoza Zaragoza Spain CSIC-Universidad de Sevilla Sevilla Spain Unitè de Gènie Enzymatique et Biologie Molèculaire Facultè des Sciences-Ain Chock Casablanca Morocco 

出 版 物：《Acta Biochimica et Biophysica Sinica》 (生物化学与生物物理学报(英文版))

年 卷 期：2003年第35卷第10期

页      面：891-896页

核心收录：

学科分类：0710[理学-生物学] 07[理学] 071003[理学-生理学] 

基　　金：ThisworkwassupportedbyAECI (Spain)  acollaborativegrantoftheAndalusianRegionalGovernment (ConvenioColaboracinUniv .Marroques grupoPAICVI 2 61)  andgrantsBMC 2 0 0 1 2 5 2andP12 0 2 0 0 1fromtheSpanishMinistryofEducationandtheDGA 

主　　题：glyceraldehyde-3-phosphate dehydrogenase hibernation thermal denaturation circular dichroism spectroscopy protein stability 

摘      要：In previous study, we demonstrated that the specific activity of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.***.1.12) in skeletal muscle of induced hibernating jerboa (hibernating GAPDH) was 3-4 folds lower than that of the one in the skeletal muscle of the euthermic jerboa (euthermic GAPDH). A significant decrease in both GAPDH protein and GapC mRNA levels occurs when hibernating, but the purified hibernating GAPDH is less active than the euthermic GAPDH. To investigate the physico-chemical basis of this lower activity, the behaviour during thermal inactivation of skeletal muscle GAPDH from hibernating and euthermic tissues was examined by a variety of spectroscopic techniques, including fluorescence emission, circular dichroism and ultraviolet absorption. A clear resistance to thermal denaturation was observed in the hibernating GAPDH compared with the euthermic GAPDH. The different temperature of denaturation found in these proteins by both fluorimetry and circular dichroism indicates that there might exist conformational changes of GAPDH upon hibernation that could affect the stability of this enzyme.