marburgensis enzyme which had negligible specific activity using NADPH compared to NADH in the presence of oxaloacetate
In the Krebs cycle, the succinate is oxidized to oxaloacetate
, producing 1 FAD[H.sub.2] and 1 NADH which produces 4 ATP in oxidative phosphorylation (steps C-6 and C-8, Figure 1).
The values of alkaline phosphatase, serum glutamate oxaloacetate
transaminase (SGOT), serum glutamate pyruvate transaminase (SGPT), albumin, and bilirubin suggested that none of the compounds had shown any considerable increase or decrease (Figure 1).
Nondiabetic Nondiabetic + HemoHIM GOT (U/L) 55 [+ or -] 7 50 [+ or -] 9 GPT (U/L) 24 [+ or -] 6 21 [+ or -] 6 LDH (U/L) 368 [+ or -] 117 301 [+ or -] 31 ALP (U/L) 124 [+ or -] 11 120 [+ or -] 10 Diabetic Diabetic + HemoHIM GOT (U/L) 126 [+ or -] 27 * 73 [+ or -] 12# GPT (U/L) 52 [+ or -] 23 * 28 [+ or -] 6 LDH (U/L) 618 [+ or -] 108 * 489 [+ or -] 112 ALP (U/L) 281 [+ or -] 56 * 193 [+ or -] 20# GOT: glutamate oxaloacetate
transaminase, GPT: glutamic pyruvic transaminase, LDH: lactate dehydrogenase, ALP: alkaline phosphatase.
Serum glutamate oxaloacetate
transaminase (SGOT) activity was found to be 13.68 [+ or -] 0.55 U/l in G1 group while in G2 and G3 groups it was increased more than six times, i.e.
(1955).Serum glutamic oxaloacetate
transaminase activity as an index of liver cell injury, a preliminary report.
[15.] Reitman S and S Frankel A colorimetric method for the determination of Serum glutamate pyruvate transaminase and serum glutamate oxaloacetate
Aspartate amino-transferes (AST) also known as glutamate oxaloacetate
transaminase (GOT) is present in heart, kidney, brain, and liver.
GOT = Glutamate Oxaloacetate
Transaminase; GPT = Glutamate Pyruvate Transaminase; ALP = Alkaline Phosphatase; G = Group; LE = Liver Enzyme
For SGOT malate dehydrogenate is used to reduce oxaloacetate
to malate where as in SGPT the pyruvate formed in the reaction is converted to lactate by lactate dehydrogenase was followed for the assessment of activity of glutamic oxaloacetic transaminase and glutamic pyruvate transaminase in the cells.
An aliquot (15 of muscle homogenate was incubated with 100 mmol/l Tris-HCl, 0.2 mmol 5,5'-dithio-bis-2-nitrobenzoic acid, 15 mmol/l acetyl-CoA, and 0.5 mmol/l oxaloacetate
, pH 8.1, at 37[degrees]C.
The activity was measured spectrophotometrically at 412 nm ([[epsilon].sub.DTNB] = 13.6 [mM.sup.-1] x [cm.sup.-1]) for 4 min in the presence of an imidazole-HCl buffer solution (100 mM; pH, 8) containing 0.1 mM 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), 0.1 mM acetylcholine A, and 0.15 mM oxaloacetate
(Thibeault et al.