With the passage of time it reached at normal concentration at 2 hours 7.50 ± 0.13 ng/ml and then declined and at last became 26.1 ± 0.15 ng/ml at eight hours. But the Tamoxifen minimum effective concentration was maintained at 6 hours where it reaches at maximum concentration 32.04 ± 0.44 ng/ml. The minimum effective concentration of the Tamoxifen in plasma was persistent during the eight hours (0.05-8.0 hours) that will assure its pharmacotherapeutic action. Cmax is defined as the maximum concentration of drug achieved in the plasma. The peak plasma concentration is the factor which depends on both the rate of drug absorption and extent of drug absorption in the plasma.
The alkaline phosphatase has a lower enzymatic activity when pH 7 and 7.5 Tris-HCl were used; whereas the enzyme has a higher enzymatic activity when pH 8, 8.5 and 9 Tris-HCl were used, with the enzymatic activity at pH 9 being the highest. This shows that the alkaline phosphatase works optimally at alkaline condition such as pH 9 (Kaslow, n.d). The results of the graph show that alkaline phosphatase work less optimally at lower pH, this may due to at lower pH, the positively-charged amino side chain of the peptide sequence of alkaline phosphatase will release the hydrogen ions, therefore causing the tertiary structure of the enzyme altered, which will causes conformation change in alkaline phosphatase’s active site. Thus, the substrate p-nitrophenyl phosphate will experience some difficulties to bind to the binding site on active site of alkaline phosphatase, therefore decreasing the enzyme activity when pH becomes
The phosphorus label is definitely not adsorbed to the proteins, since the entire orthophosphate radioactivity added to the isolated synaptosomal fraction remains acid soluble. The finding that RNase does not release radioactivity from the synaptosomes-enriched fraction indicates that the preparation is not contaminated with free polyribosomes. Pronase appears to render the radioactivity from both the whole synaptosome-enriched and the final phosphoprotein residue ( Table 2 ) acid soluble, indicating that the label is initially attached to amino acids. Solubilization by alkaline phosphatase digestion proves that the phosphate is indeed covalently bound. Tryptic digestion of the final phosphoprotein residue and detection of the increased phosphorylation in the ninhydrin-staining band of peptides derived from synaptosomes of trained mice is further evidence of this.
The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds. It was hypothesized that the optimal pH for the enzyme was pH 7 while the 1.0 ml peroxidase would have the best reaction rate. At the end of the experiment the results prove the hypothesis to be incorrect. INTRODUCTION Enzymes are proteins that allow a reaction to speed up. These proteins are made up of monomers known as amino acids.
It has been reported that gastric lipase in humans show a selectivity for hydrolysis mainly towards sn-3 position, followed by favoring sn-1 position . As human gastric lipase is active in a broad pH range of 2-7 with an optimum pH range between 4.5 and 5.5, it continues to contribute to lipid digestion through the duodenum . In humans, the lipid digestion resulting from the stomach is responsible for about 10-30% of the hydrolysis of dietary fat which suggests that majority of the hydrolysis of fats occurs in the intestine mediated by pancreatic lipase [48, 51]. Pancreatic lipase also known as pancreatic triacylglyceride lipase preferentially hydrolyzes triacylglycerides at 1 and 3 positions yielding 2-monoglyceride and two FAs for every triacylglyceride molecule it hydrolyzes (Figure 8) [54, 55]. Figure 8: Hydrolysis of triacylglycerols by pancreatic lipase (modified from ) The optimal activity of pancreatic lipase is between pH 6.5 to 8.0 .
A peroxidase is an enzyme that acts as catalysts, which occurs in biological systems. Peroxidase is found in plants, which they play a role in helping to minimize damage caused by stress factors or insect pests. Along with being found in plants, they are also present in liver cells, kidney cells, leukocytes and erythrocytes. For the concentration of enzyme experiment, the hypothesis was if the concentration of an enzyme increases, then the enzyme activity will increase as well. The hypothesis was proven to be true, because there are more enzymes to react with substrates.
The melting point of the experimentally synthesized Aspirin product was found to be between 126-129 ˚C. This temperature range of initial to final melting point has a small and sharp temperature range of only 3˚C, which is within the acceptable limits of the 128-137˚C1 literature value for Aspirin (Acetylsalicylic Acid/2-acetoxybenzoic acid), if located slightly toward the beginning of the literature melting temperature range. Therefore, the narrow melting point range, which falls within the standard literature value range results, indicate the reliability purity of the sample. Had the melting point been higher than the literature value, but maintained a sharp melting point range, the compound could have still indicated a pure sample. A lower
Aim of this investigation is to find out how much of an effect there is on enzyme activity and reaction time as pH values change. In this practical, the enzyme that will be used for experimentation purposes is catalase. This molecule is usually found in animal and potato cells, and a substantial amount can be found in any potato extract. The substrate that will be catalyzed is hydrogen peroxide (H2O2,), a common but toxic end product of our metabolism, and highly dangerous if accumulated in the body and not decomposed. It can damage cells if it is not removed.
First, blood pH should be kept in a narrow range for different enzymes and other components of the blood to function. If blood pH is too high or too low, it can cause problems with the health of a person, including seizures, coma and even death. Second, a person’s blood pH within the clinical range of 7.37-7.43, but they can close one of these extremes, and eating the “wrong” foods may push them further from the optimum pH of 7.40. The good news is that once a person knows and understands their metabolic type, they can be a nutrition plan to help balance their blood pH to the optimum