Different Thermostability of Skeletal Muscle Glyceraldehyde-3-phosphate Dehydrogenase from

Different Thermostability of Skeletal Muscle Glyceraldehyde-3-phosphate Dehydrogenase from

Hibernating and Euthermic Jerboa (Jaculus

orientalis)

IDDAR Abdelghani;CAMPOS Luis A.;SANCHO Javier;SERRANO Aurelio;SOUKRI Abdelaziz

【期刊名称】《生物化学与生物物理学报：英文版》 【年(卷),期】2003(035)010

【摘要】In previous study, we demonstrated that the specific activity of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) 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