The effect of albumin administration on renal dysfunction after experimental surgical obstructive jaundice in male rats

AbstractThe aim was to study the influence of albumin supplementation on the changes of the kidney function and structure in cirrhotic rats induced by common bile duct ligation (BDL). Twenty-four male albino rats weighing 200–250g were divided into Group I: 6 rats underwent laparotomy alone, and the bile duct was only dissected from the surrounding tissue; Group II: 6 rats underwent a sham operation and received 2% albumin in their drinking water; Group III: 6 rats were subjected to bile duct ligation only; and Group IV: 6 rats were subjected to bile duct ligation and received a daily albumin 2% in drinking water. All rats were sacrificed after 4 weeks. We measured the liver and kidney functions and oxidative stress markers in the renal tissue and conducted a histological evaluation of the liver and kidney. The liver enzymes were decreased, but there was no significant difference in the bilirubin levels in group IV compared to group III. There was a significant elevation of serum creatinine in group III compared to group II, and serum creatinine was attenuated in group IV. The renal tissue catalase activity and reduced glutathione, as well as the nitric oxide levels, were significantly increased in group IV and were elevated in group III. Histologically, the livers of group IV showed degeneration and inflammatory cell infiltration with regeneration areas in which normal hepatocytes appeared. The kidneys of group IV showed recovery as well as areas of inflammatory cell infiltration. Some tubules appeared with normal epithelial lining. In conclusion, the results suggest that albumin partially improves the renal functions and structures after their disturbances as a result of BDL

Molecular docking studies of Meso-tartrate and Diiodophenylpyruvate enzymes

Oxidoreductases are enzymes that catalyze the oxidation of one molecule to another using NAD+ and NADP as co-factors. In this study, homology modeling and/or molecular docking are done for two selected homosapian enzymes Malate dehydrogenase (Uniprot ID: MDH1) and Homosapian alcohol dehydrogenase (1U3U). The homology modeling for Malate dehydrogenase was built in comparison with its porcine analog (5MDH) using SWISS-MODEL. Its active site was determined by aligning with the 5MDH template using PyMol. Homosapian alcohol dehydrogenase (1U3U) was selected as target crystal structure based on its specific criteria (resolution 1.60 Å, Rfree value 0.186, Ramachandran outliers value 0), and prepared with AutoDock. Its active site was determined using AutoDock grid tool. The co-crystallized ligand was prepared using open babel. Molecular docking was done for both enzymes, and five ligands from 89 ligands are the best results obtained based on their binding configuration and binding affinity using Autodock Vina