scholarly journals Chemical detections of active compounds in Melilotus indica extracts

2009 ◽  
Vol 3 (1) ◽  
pp. 130-140
Author(s):  
Faisal K. Mutasher ◽  
Ghazi M. Aziz ◽  
Amani A.W . Abdul-Razzak
Keyword(s):  
Phosphate Buffer ◽  
Volatile Oils ◽  
Buffer Solution ◽  
Active Compounds ◽  
Buffer Solutions ◽  
Negative Results ◽  
Sodium Phosphate Buffer ◽  
Crude Extracts ◽  
Layer Chromatography ◽  
Positive Results

The crude extracts of the leaves of melilotus indica which collected in two dates (midFebruary, mid March) have been prepared by three solvents (Distilled water, ethanol 80% and chloroform) and three buffer solutions (Sodium acetate buffer, Sodium phosphate buffer and Tris-hydrochloric acid buffer), the greater percentage of crude extracts achieved by phosphate buffer which were 47.3% and 29.2% for second and first dates, respectively, while the lowest percentage of crude extracts achieved by chloroform extracts which were 13.2% and 10.0% for second and first dates, respectively. The qualitative chemical detections for active compounds in crude extracts revealed a positive results for the saponins, tannins, coumarins, flavones and glycosides, while the detections revealed a negative results for the alkaloids, resins and volatile oils. The active compounds in crude extracts prepared by solvents and buffer solutions were studied by thin layer chromatography (TLC), the solvent extracts were contains five compounds with relative flow (RF) 0.65, 0.4 for coumarin and umbelliferon, respectively, and 0.5, 0.27, 0.2 which belong to simple coumarins compounds in melilotus indica, while buffer solution extracts were contains two compounds with RF value 0.65 and 0.4 for coumarin and umbelliferon, respectively.

scholarly journals Analisis Antalgin dalam Jamu Pegal Linu yang Dijual di Pasar Beringharjo Yogyakarta

2017 ◽  
Vol 4 (1) ◽  
pp. 29
Author(s):  
Siti Fatimah ◽  
Muji Rahayu ◽  
Debi Firma Indari
Keyword(s):  
Herbal Medicine ◽  
Traditional Medicine ◽  
Plant Material ◽  
Diclofenac Sodium ◽  
Research Data ◽  
Negative Results ◽  
Traditional Market ◽  
Animal Material ◽  
Layer Chromatography ◽  
Positive Results

Background: Traditional medicine is an ingredient or ingredients in the form of plant material, animal material, mineral materials, preparation essence (galenic), or mixtures of these materials that have historically been used for treatment, and can be applied according to the prevailing norms in society. Traditional medicine  is often chosen as a remedy for health care is herbal, because herbal medicine is a health drink. Chemicals drugs were added by the makers of herbal medicine with the intent may be to increase the efficacy of herbal medicine and herbal medicine provide more instant effect, it is becoming a source of danger herbs. BPOM many find herbs aching pains who defiled chemical medicines like phenylbutazone, methampyrone, diclofenac sodium, piroxicam, paracetamol, prednisone, or dexamethasone. Chemicals a drug it is set in PERMENKES 007 of 2012. Methods: This research is to describe the whether or not of chemicals in the antalgin sold in the Beringharjo traditional market Yogyakarta. The method used to test the lab using thin layer chromatography. Research data presented in terms of percent. Results: Research is obtained value Rf sample 0.63 until 0.8 one sampel having the value Rf and fluorescence equal to standard methampyrone. Value Rf standard methampyrone 0,78 and red purple fluorescence. Conclusion: There are methampyrone in herbal medicine aching pains sold in the Beringharjo traditional market to a presentation positive results as many 8.3%  and negative results 91.7%.

scholarly journals THE PROPERTIES OF MAMMALIAN STRIATED MYOFIBRILS ISOLATED BY AN ENZYMATIC METHOD

1950 ◽  
Vol 91 (6) ◽  
pp. 655-664 ◽  
Author(s):  
Armin F. Schick ◽  
George M. Hass
Keyword(s):  
Ionic Strength ◽  
Potassium Chloride ◽  
Phosphate Buffer ◽  
Phosphate Buffer Solution ◽  
Potassium Phosphate ◽  
Microscopic Structure ◽  
Buffer Solution ◽  
Buffer Solutions ◽  
Alkaline Side ◽  
Fresh Frozen

A new method for the isolation of large numbers of individual myofibrils from fresh mammalian skeletal and cardiac muscle has been described. Purification of isolated myofibrils was accomplished by differential centrifugation of fresh frozen sections of muscle which had been mechanically agitated after exposure for 30 to 45 minutes at 0°C. to the action of a dilute solution of trypsin in a phosphate buffer solution with a pH of 7.0 and an ionic strength of 0.25. Isolated skeletal myofibrils of the rabbit and man have similar constant solubility properties. They dissolve in an aqueous mixture of 0.5 N potassium chloride and 0.03 N sodium bicarbonate, giving viscous solutions which exhibit conspicuous birefringence of flow. They are soluble in buffer solutions (ionic strength 0.15) on the acid side of pH 4 and alkaline side of pH 10. If the ionic strength of potassium phosphate buffer solutions is increased to 0.5 or if the ionic strength of phosphate-borate buffer solutions is increased to a similar value by addition of potassium chloride, the isolated myofibrils become soluble at neutrality. Hence, it is possible, first to isolate the myofibrils and then dissolve them without deviating appreciably from physiologic ranges of pH. The extent to which myofibrils are modified by the conditions imposed by the method of isolation is unknown. There is no significant change in microscopic structure or optical birefringence. Furthermore, there is retention of a form of physiological reactivity, for when the isolated skeletal myofibrils are immersed in solutions of adenosinetriphosphate, they promptly and irreversibly change from elongated fibrils with distinct structural detail into dense spherical masses without recognizable microscopic structure.

scholarly journals The Influence of Phosphate Buffer on the Formation of N-Nitrosodimethylamine from Dimethylamine Nitrosation

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Long Xu ◽  
Zhi Sun ◽  
Qing Ming Liu ◽  
Yong Dong Liu ◽  
Ru Gang Zhong ◽  
...  
Keyword(s):  
Significant Role ◽  
Phosphate Buffer ◽  
Inhibitory Effect ◽  
Buffer Solution ◽  
Citrate Buffer ◽  
Buffer Solutions ◽  
Water Plants ◽  
Almost All ◽  
Nitrosation Reaction

Buffer solutions were widely used for almost all the investigations concerning N-nitrosodimethylamine (NDMA), a member of powerful mutagenic and carcinogenic compounds which are ubiquitous in the environment. However, whether or how the buffer matrixes influence NDMA formation is still unknown. The effect of buffer solutions on NDMA formation from the nitrosation of dimethylamine (DMA) by nitrite (NaNO2) was investigated at pH 6.4 in four kinds of buffer solutions, that is, Na2HPO4/C6H8O7, Na3(C6H5O7)/C6H8O7, NaH2PO4/NaOH, and NaH2PO4/Na2HPO4. Our observations demonstrate an unexpected inhibitory effect of the buffer solutions on NDMA formation and the phosphate buffer plays a more significant role in inhibiting NDMA formation compared to the citrate buffer. Moreover, the amount of the phosphate in the buffer was also found to greatly impact the formation of NDMA. A further investigation indicates that it is the interaction between NaH2PO4and reactant NaNO2rather than DMA that leads to the inhibitory effect of phosphate buffer during the DMA nitrosation reaction. This study expands the understanding of the influence of buffer solution on nitrosamines formation through the nitrosation pathway and further gives a hint for water plants to reduce the formation of nitrosamines.

scholarly journals Effect of combination of electrolyte and buffer on electrical production in fuel cell microbial system with Pseudomonas sp. in molasses substrate

2020 ◽  
Vol 211 ◽  
pp. 03001
Author(s):  
Maswati Baharuddin ◽  
Muh Rajib ◽  
Sappewali ◽  
Ummi Zahra
Keyword(s):  
Electrolyte Solution ◽  
Phosphate Buffer ◽  
Phosphate Buffer Solution ◽  
Potassium Phosphate ◽  
Salt Bridge ◽  
High Energy ◽  
Pseudomonas Sp ◽  
Buffer Solution ◽  
Sodium Phosphate Buffer ◽  
Potassium Phosphate Buffer Solution

MFC is a bio-electrochemical system driving an electric current by using high-energy bacteria and oxidants. This research aimed to investigate the effect of electrolyte and buffer on electrical production using Pseudomonas sp. In Molasses substrate. The method in this research was the double compartment that consist of anode and cathode chambers. Both were related by salt bridge. This study showed that the addition of a combination of KMnO4 electrolyte solution with sodium phosphate buffer solution obtained a maximum potential difference of 0.67 V. The result also revealed that the combination of KMnO4 electrolyte solution with Potassium Phosphate Buffer solution produced a 1.44 mA maximum current with power density of 660.82 mW/m2.

scholarly journals Crosslinking Efficacy and Cytotoxicity of Genipin and Its Activated Form Prepared by Warming It in a Phosphate Buffer: A Comparative Study

Materials ◽  
2021 ◽  
Vol 14 (21) ◽  
pp. 6600
Author(s):  
Takeya Kawamura ◽  
Shunji Yunoki ◽  
Yoshimi Ohyabu ◽  
Toshio Uraoka ◽  
Kazuaki Muramatsu
Keyword(s):  
Phosphate Buffer ◽  
Phosphate Buffer Solution ◽  
Mechanical Tests ◽  
Buffer Solution ◽  
Sodium Phosphate Buffer ◽  
In Situ Forming ◽  
Custom Made ◽  
Acute Cytotoxicity ◽  
Sodium Phosphate Buffer Solution

The aim of the present study was to compare the acute and cumulative cytotoxicity of intact (n-GE) and warmed genipin (w-GE), while investigating the differences in crosslinking capabilities of these two genipins by rheological and mechanical tests. The n-GE solution was prepared by dissolving genipin powder in a sodium phosphate buffer solution. The w-GE solution was prepared by warming the n-GE solution at 37 °C for 24 h. The mechanical tests for chitosan (CH)/genipin gels showed the crosslinking rate of w-GE was much greater than that of n-GE up until 6 h after preparation, whereas the degree of crosslinking of CH/n-GE gels became higher at 12 h. The ISO 10993-5 standard method, which is established specifically for evaluating cumulative cytotoxicity, determined equivalent IC50 for w-GE (0.173 mM) and n-GE (0.166 mM). On the other hand, custom-made cytotoxicity tests using a WST-8 assay after 1 h of cultivation showed that the acute cytotoxicity of w-GE was significantly higher than that of n-GE at concentrations between 0.1–5 mM. The acute cytotoxicity of w-GE should be taken into consideration in its practical uses, despite the fact that the much faster crosslinking of w-GE is useful as an effective cross linker for in-situ forming gels.

scholarly journals Investigation of guanidine hydrochloride induced unfolding of apolipoprotein A-IMilano

2002 ◽  
Vol 16 (3-4) ◽  
pp. 199-206 ◽  
Author(s):  
Malin Suurkuusk ◽  
Dan Hallén
Keyword(s):  
Phosphate Buffer ◽  
Sodium Phosphate ◽  
Guanidine Hydrochloride ◽  
Phosphate Buffer Solution ◽  
Buffer Solution ◽  
Unfolded Protein ◽  
Sodium Phosphate Buffer ◽  
Apolipoprotein A ◽  
Helical Content ◽  
Sodium Phosphate Buffer Solution

A guanidine hydrochloride (GuHCl) induced unfolding study of apolipoprotein A-IMilano(apo A-IM) has been performed. The unfolding was followed by circular dichroism (CD) measurements at 222 nm and by isothermal titration (ITC) calorimetry at 25°C. In the ITC experiments enthalpies of transfer were determined for apo A-IMfrom aqueous sodium phosphate buffer solution into solutions of different concentrations of GuHCl. The CD data and the ITC data give complementary and consistent results of the complex unfolding process. Analytical ultracentrifugation experiments were made on apo A-IMin sodium phosphate buffer and in 0.6 M GuHCl, respectively. Analyses of the obtained sedimentation velocity data show that apo A-IMis highly aggregated in sodium phosphate buffer. The aggregates are almost completely dissociated in 0.6 M GuHCl. Aggregation of the protein in sodium phosphate buffer solution induces an increase in α-helical content. The loss of α-helical secondary structural element of the protein upon dissociation of the aggregates destabilises the protein resulting in a low GuHCl concentration of unfolding, [GuHCl]m=1.1 M. The unfolded protein has a significant α-helical content at the unfolded state. From ITC- and CD data we suggest that increased binding of GuHCl to the unfolded protein results in a disruption of the residual secondary structure.

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