DIFFERENTIAL ACTIVITIES OF ISOCITRATE DEHIDROGENASE IN PORCINE COCS

ELIZABETH BREININGER; GABRIEL MARTIN ALVAREZ; CYNTHIA GUTNISKY; PABLO DANIEL CETICA

Chascomus

Jornada; XVI Jornadas de la Sociedad Argentina de Biología; 2014

Sociedad Argentina de Biología

Our aim was to determine the activity of NAD and NADP dependent isoenzymes of isocitrate dehydrogenase (IDH) in immature or in vitro matured cumulus-oocyte complexes (COCs). IVM was carried out during 48 h, 39ºC, 5% CO2 in medium 199 with gonadotropins. COCs were sonicated (4 min) and centrifuged (17000xg, 20 min), being the activity determined in the supernatant. An enzymatic unit (U) was defined as the amount of enzyme necessary to form 1 µmol of NAD (P). Enzymatic activity was expressed in U (U/COC) and specific activity (U/mg protein) as mean±SEM and compared by Student?s t test. For the NAD isoenzyme the U was (3.56±0.56) 10-6 and (2.67±0.36) 10-6, for immature and matured COCs, respectively. In NADP isoenzyme U was (2.81±0.64) 10-5 and (2.90±0.84) 10-5, for immature and matured COCs, respectively. The specific activity in the NAD isoenzyme was (6.05±1.28) 10-4 and (1.51±0.20) 10-4, for immature and matured COCs, respectively. In NADP isoenzyme the specific activity was (1.19±0.43) 10-2 and (0.64±0.23) 10-2, for immature and matured COCs, respectively. A significant decrease (p