The complexes of Pd+2 ion with 2-(5-bromo-2-pyridylazo)-5-dieıhyl aminophenol (BPADAP) were studied kinetically and spectrophotometrically in aqueous ethanolic solutions. The reagent forms 1:1, 2:1 square planer and 1:1 bridged shape binuclear complexes with Pd+2 ion. All these complexes (violet colour) absorb light in the same region at 540, 575 and 618nm. The band at 618 nm seems to be specific for complexes of Pd+2ion with BPADAP.   The rate constants of the growth in 93% H2O + 7% ethanol of 1:1 and 2:1 complexes at 575 and 618 nm were followed the first order kinetics and are quite of the same values , 0.495 and 0.463 min- 1  respectively. The rate constants of the decay of 2:1 complex

Background: Diabetes is a metabolic disorder characterized by chronic hyperglycemia due to an inability to produce insulin. Uncontrolled or poorly controlled diabetes is clinically associated with increased susceptibility to delay healing. Many recent researches have shown that stem cell therapy can be the best choice for treatment of this disease. The aims of this research were investigating regeneration of pancreatic beta cells of diabetic induced rabbits after stem cell transplantation. Materials and Methods: 64 rabbits weighting an average of (2.5 - 3 kg) were used in this experimental study, and divided into 4 groups as follows; group A ( contains 16 healthy rabbits regarded as control group ) , Group B ( contains 16 diabetic rabbits

Mefenamic acid was esterified with starchwith[1:1] Molar ratio, as drug substituted with natural polymer, to prolongthe period of hydrolysis of drug polymer with other advantages. The new prodrug starch was characterized by FT-IR and UV-Visible and 1H-NMR spectroscopies. The physical properties were studied and controlled drug release was studied in different pH values at 37oC. The stability of drug was carried out by measuring the absorbance of mefenamic starch which hydrolyzed in HCl solution of pH 1.1 (artificial gastric fluid) and phosphate buffer of pH 7.4 (simulating intestinal fluid SIF) at 37oC for several days. The thermal analysis such as DSC was studied.

The efficiency of attapulgite liners as anti-seepage for crude oil is examined. Consideration is given to the potential use of raw attapulgite and mixture attapulgite with prairie hay and coconut husk as liners to prevent crude oil seepage. Attapulgite clay used in this study was brought from Injana formation /Western Desert of Iraq. Two types of Crude oil brought from Iraqi oil fields were used in experiments; heavy crude oil from East-Baghdad oil field and light crude oil from Nassiriya oil field. Initially the basic properties of attapulgite and crude oils were determined. The attapulgite clay was subjected to mineralogical, chemical and scanning electron microscope analyses. Raw Attapulgite 150µm, 75µm, and 53µm were tested

Azithromycin is the drug of choice in the treatment of several bacterial infections, most often those causing middle ear infection, bronchitis, pneumonia, typhoid and sinusitis. It’s also effective against certain urinary tract infections and venereal diseases. This study was carried out to prepare an acceptable suspension either as dry physical mixture powder or granules to be reconstituted, through studying the effect of various type and concentration of suspending agent (xanthan gum, hydroxypropyl methylcellulose (HPMC), either alone or in combination) on the release profile of the drug. The best prepared suspension formulas (H& III) were selected depending on the dissolution profile of each formulas and then compared with

In this study , the effect of an organic compound prepared as derivative of oxazepine tested on the activities of aspartate amino trasferase (AST) and alanin amino transferase (ALT). The kinetic study of such enzymes is in the presence of oxazepine derivative.  The results revealed that the organic compound is a non competitive inhibitor for both enzymes.  The Km value for AST is 1.3 × 10-3 M and Vmax for the uninhibited is 200 U/mL and for the inhibited is 111.1 U/mL while Km value for ALT is 2.5 × 10-3 M and Vmax are 89.66 U/mL and 56.77 U/mL for the uninhibited and inhibited enzyme respectively.