Biochemistry
Pooyan Pedram; Mohammad Fazilati; Marzieh Rashidipour; Habibollah Nazem
Abstract
Lactate dehydrogenase (LDH) is a key enzyme in cellular metabolism found in all animals. It plays a crucial role in converting pyruvate to lactate and vice versa. LDH is present in a wide range of tissues and cells in the animal body. In recent decades, nanoparticles have been utilized due to their unique ...
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Lactate dehydrogenase (LDH) is a key enzyme in cellular metabolism found in all animals. It plays a crucial role in converting pyruvate to lactate and vice versa. LDH is present in a wide range of tissues and cells in the animal body. In recent decades, nanoparticles have been utilized due to their unique properties for designing optical and electronic sensors. This research presents a novel colorimetric method: silver nanoparticles synthesized using chrysanthemum aqueous extract are employed for direct detection of lactate dehydrogenase activity. Initially, chrysanthemums were collected from greenhouses in Mahallat County under the supervision of experts. After separation and powder preparation of the flower part of the plant, chrysanthemum aqueous extract was prepared. Subsequently, the synthesis of silver nanoparticles using aqueous extract and addition of silver nitrate solution was investigated by optimizing appropriate conditions. In the next step, two vials were prepared, each containing a reaction mixture comprising Tris-HCl, MgCl2, and NADH. Additionally, one vial contained LDH. Silver nanoparticles and sodium borohydride were then added to the vials. The enzyme can convert NAD+ to NADH. The detection mechanism of lactate dehydrogenase enzyme is based on the aggregation of silver nanoparticles, which leads to an increase in their size and consequently a color change. Thus, the presence or absence of the enzyme can be easily distinguished with the naked eye in a single step. In the presence of the enzyme, the color of the solution used in the study was yellow, while in the absence of the enzyme, the color was grayish. Consequently, lactate dehydrogenase enzyme can be identified with high sensitivity.
Biochemistry
Ali Ahmadi Shapourabadi; Mohammad Fazilati; Habib-Allah Nazem
Abstract
Lactoferrin is one of the milk proteins that has shown a wide range of physiological activities such as antibacterial, anti-protozoal, anti-fungal, anti-viral, anti-cancer, antioxidant, anti-inflammatory and immunomodulatory. In this study, lactoferrin was extracted and purified from cow, sheep and goat ...
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Lactoferrin is one of the milk proteins that has shown a wide range of physiological activities such as antibacterial, anti-protozoal, anti-fungal, anti-viral, anti-cancer, antioxidant, anti-inflammatory and immunomodulatory. In this study, lactoferrin was extracted and purified from cow, sheep and goat milk. HPLC analysis and determination of the concentration of these three extracted lactoferrins were performed. Antibacterial activity against Gram negative Escherichia coli and Salmonella typhi and gram positive Bacillus cereus and Staphylococcus aureus and antioxidant activity were investigated. The activity of lactoferrin against DPPH free radical was investigated. Also, lactoferrin activity was evaluated in neutral acidic and alkaline environments. The combination test with iron was also performed with FeNTA reagent. The findings showed that lactoferrin has the ability to inhibit two bacteria, Escherichia coli and Staphylococcus aureus. Also, the evaluation of lactoferrin activity in neutral acidic and alkaline environments showed that lactoferrin is more stable in alkaline environment than other environments. In the combination test with iron, the results indicated the combination of lactoferrin with iron. The percentage of free radical inhibition was equal to %4.49. Also, the results showed that the concentration of lactoferrin in goat's milk is higher than that of sheep's and cow's milk and its amount was equal to 131.66 μg/ml.
Gholamreza Mahdieh najafabady; Mohammad Fazilati; Aliasghar Pilehvarian; Habib olah Nazem
Abstract
Abstract High blood pressure doubles the risk of cardiovascular disease. In addition to chemical drugs, biodegradable peptides have antihypertensive properties and the Ile-Gln-Pro peptide is one of these peptides. Spirulina is a green-blue algae of the cyanobacteria branch, which is now used as a supplement ...
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Abstract High blood pressure doubles the risk of cardiovascular disease. In addition to chemical drugs, biodegradable peptides have antihypertensive properties and the Ile-Gln-Pro peptide is one of these peptides. Spirulina is a green-blue algae of the cyanobacteria branch, which is now used as a supplement to the pharmaceutical industry. The Ile-Gln-Pro peptide was extracted from Spirulina platensis algae using an alkalase enzyme and was analyzed by filtration gel chromatography and RP-HPLC and its inhibitory effect on the ACE enzyme was investigated. ACE enzyme was inhibited by Ile-Gln-Pro peptide by non-competitive inhibition method with Ki = 5.8 μM and IC50 = 0.65 μM . According to the available information from the ACE inhibitor peptide in the BIOPEP database, a comparative study was performed on the location of amino acids in the ACE inhibitor peptide and its effect on the potency of tri-peptide inhibition. Based on SPSS software, on the 196 ACE inhibitor peptide, the presence of Lys, Gly, Thr and Pro amino acids at the end of C and His, Ala, and Met amino acids at the end of N, as well as Phe, Ala, His And His in the middle of peptide have relationship with EC50 and peptide-inhibiting potency.
