Cure Tooth Decay Heal And Prevent Cavities With Nutrition

About seven months ago, I walked out of a dental office with a pretty serious quote for dental work that was needed to be done on 8 different cavities they found in my teeth. I was confused. I eat a pretty good diet. How could my teeth have cavities? I brush and I floss every day. How could this happen? I told my dentist that I had heard about the â€Å"remineralization† of teeth and even curing tooth decay and cavities with certain staples in your diet, and asked him his opinion on the subject. Of course, like any conventional dentist, he had never heard of it. I’m pretty sure he even offered fluoride treatments at that point. After that, I stopped asking questions, scheduled an appointment to have all of the cavities filled, and left somewhat upset and unsatisfied. When I got home, I began researching natural ways to heal your teeth. I read the book â€Å"Cure Tooth Decay: Heal Prevent Cavities with Nutrition† by Ramiel Nagel, and learned about healing and remineralization of teeth with a good diet, and my mind was completely blown. I can actually heal my own cavities without spending thousands at the dentist? I can actually heal my cavities and remineralize my teeth with a proper diet? No more needles or drills in my mouth? Count me in! To completely understand how to heal your own cavities, we need to look at what causes tooth decay. Lack of Nutrition is the Root of Tooth Decay Dr. Weston A. Price, who is a prominent dentist and author of â€Å"Nutrition and PhysicalShow MoreRelatedDental Question Bank33485 Words   |  134 Pagesclass V abrasion cavity with GIC you should A. B. C. Clean with pumice, rubber cup, water and weak acid Dry the cavity thoroughly before doing anything Acid itch cavity then dry thoroughly 4. Which of the following statement about the defective margins of amalgam restoration is true? A. The larger the breakdown, the greater the chance of decay. 5. The retention Pin in an amalgam restoration should be placed A. B. Parallel to the outer wall Parallel to the long axis of tooth 6. The most common

University Of Washington And I Am From Malaysia, A...

I study in University of Washington and I am from Malaysia, a multicultural country. Over the past four years of being away from home, I have grown and improved a lot. Coming from a multicultural country, I am fluent in English, Malay, Mandarin, and Cantonese and I can be a linguistic to overcome the language barrier in the University of California – Santa Barbara (UCSB)’s community. My knowledge of different cultures and religions will promote mutual understanding in the community. I can adapt into new environment smoothly and I can help others to blend into new environment as well. Therefore, I learn empathy and understand people from their perspectives. My experience in helping my brother to battle with depression further instills empathy in me. Thus, I can be a cultural navigator to help people to see in others perspective and a good listener. Therefore, based on my cultural background and life experiences, I will increase productivity, promote mutual understanding, foster good mental development within the UCSB community. By joining the UCSB’s community, I can be a linguistic. I am fluent in English, Mandarin, Cantonese, and Malay. Furthermore, I am still learning Japanese in UW. I am aware that language barrier is common especially in the Physics department where people from the world gather to do Physics. I work in the UW Trapped Ion Quantum Computing Lab. I sense there is a huge barrier between non-English native speakers and English native speakers. Non-EnglishShow MoreRelatedPsychobiography on Nelson Mandela2020 Words   |  9 PagesPersonality Dimensions developed by Paul Costa and Robert McCrae. Nelson Mandela was a well-known South African politician, philanthropist, and an anti-apartheid revolutionary, born on eighteenth of July 1918. He served as the South African President from the year 1944 to 1999. 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LDH Purification lab Report free essay sample

Abstract The enzyme lactate dehydrogenase (LDH) catalyzes the last step of anaerobic glycolysis that is important for the normal function of the body. Purification of LDH is essential to understand its structure and function. The purpose of this experiment was to extract and purify LDH enzyme from chicken muscle tissue using a variety of various. Analytical methods such as activity and protein assay were employed to determine the presence and purity of LDH. The cells were initially disrupted and proteins were solubilized. LDH was purified from the ammonium sulfate precipitated protein mixture by affinity chromatography and its activity was studied by spectrophotometric determination of NADH at 340 nm. From Pierce BCA assay of crude homogenate, initial protein concentration was shown to be 100 mg/ml. The final protein concentration of the pooled affinity sample was shown to be 0.2 mg/ml. It was found that the total specific activity of LDH was 58.5  µmol/min/mg, and yield of 0. 6%. Even though we were successful in purifying LDH enzyme, further steps can be taken to increase the yield. Materials and Methods Cell Lysis and Extraction of LDH: Approximately 40 g of minced chicken breast meat (40.327 g) is blended with 75ml cold extraction buffer in four 30-seconds bursts for homogenation of the muscle tissue. The extraction buffer contained 10mM Tris-HCl (pH-7.4), 1mM 2-Mercaptoethanol, 1mM Phenylmethylsulfonylflouride (PMSF), 1mM Ethylene diamine tetraacetic acid (EDTA). The homogenization procedure was carried out in the cold room to prevent the denaturation of proteins. The homogenate was centrifuged at 15,000 rpm for 20 minutes at 40 C. The supernatant was filtered through two layers of cheesecloth to remove lipids from the supernatant. The total volume was noted and three 0.5 ml aliquots (crude extract) were stored at -200 C. Ammonium sulfate precipitation: 60% ammonium sulfate concentration was used to precipitate proteins. 0.39 g of ammonium sulfate per ml of the  supernatant was added gradually to the supernatant for 15-20 min with continuous gentle stirring at 40 C. The mixture was centrifuged for 20 minutes at 15,000 rpm at 40 C. The supernatant was discarded and the pellet was stored at -200 C. Dialysis: Ammonium precipitation leads to high concentration of salts in protein mixture that can interfere with further purification steps. In order to remove excess salts, dialysis was performed. The pellet was suspended in Tris-PMSF buffer (10 mM Tris-HCl, pH 8.6, 0.5 mM 2-Mercaptoethanol, and 1mM ratio of EDTA) and mixed very gently until it dissolved at 40 C. Volume of 4ml protein mixture was added in the dialysis tubing and incubated twice overnight with two 1L buffer changes (Same buffer as extraction buffer that was used for cell lysis). After two incubations, protein mixture was resuspended gently and centrifuged for 10 minutes at 15,000rpm at 40C. Pellet was discarded, total volume of supernatant was noted and three 0.1 ml aliquots were collected. Affinity Chromatography: Cibarcon Blue column was used to separate LDH from the other proteins. 5ml fractions were collected in thirteen test tubes. Column was first rinsed with Tris-PMSF buffer followed by addition of protein mixture. Then, 10ml NAD Buffer (10mM Tris-HCl pH-8.6, 0.5mM 2-Mercaptoethanol, 1mM Lithium acetate and 1mM NAD+) was added followed by 10ml NADH (10mM Tis-HCL PH 8.6, 1mM NADH and 0.5mM 2-Mercaptoethanol). Between each steps, column was washed with 10ml Tris-PMSF Buffer. Each fraction was subjected to absorbance reading of 280nm. For absorbance above 1.5nm, 1:10 dilutions were carried out. Activity Assay: We used LDH Enzyme assay to measure the amount of LDH activity in our protein mixture. LDH catalyzes the conversion of lactate to pyruvate and NAD+ to NADH. The NADH can be determined spectrophotometrically at 340 nm. The LDH assay was performed in the crude homogenate, desalted fraction and six peak fractions from the Cibacron blue column. A cocktail solution was prepared by mixing lactate stock solution (120 mM lithium lactate, 10 mM Tris-HCl; pH 8.6), NAD+ stock solution (12 mM NAD+, 10 mM Tris HCl; pH 8.6) and bicarbonate stock solution (18 mM NaHCO3, 0.5 M NaCl)  in the ratio of 6:4:2 in cuvette. 10 microliters of the sample is then added and the assay absorption is measured at 340nm. If absorbance was above 1.5, samples were diluted. Protein Assay: The Pierce BCA Protein Assay (Thermo Scientific) is a detergent-compatible formulation based on bicinchoninic acid (BCA) for the colorimetric detection and quantitation of total protein concentration. A series of standard solution of Bovine Serum Albumin (BSA) ranging from 0-2000  µg/ml was prepared from a stock solution of 2 mg/ml BSA. 25ul of diluted crude (1:500, 1:250), desalted (1:100, 1:50), and 6 peak fractions from cibarcon blue column (1:10, 1:5) were loaded in microplate along with 175ul of BCA working reagent. Microplate was incubated for 30min at 370C and then the absorbance was measured at 562nm. Results/Discussion The purpose of this experiment was to extract and purify LDH enzyme from chicken muscle tissue using a variety of techniques including homogenization, ammonium sulfate precipitation, dialysis, and affinity chromatography. Activity and Protein assay were used to track the overall amount of LDH present in the samples. Crude Extraction: Chicken muscle tissue was homogenized in a blender with cold extraction buffer in order to lyse cells, releasing LDH into slurry of tissue components. Centrifugation separated membranes, nuclei, and other large cellular components to a pellet leaving a supernatant of crude product. Controlling temperature was a major consideration after homogenization since not only did this step releases proteins like LDH from the cell, but it also releases proteases that can now interact to degrade the LDH. Keeping samples on ice, pre-cooling the buffer, and avoiding excess kinetic energy through conservative blending were methods used to minimize activity of these proteases. After filtration through cheesecloth, our final volume of crude homogenate sample 74ml, much more volume than expected. Addition of more than 75ml of buffer volume could have increased the volume. Other possible explanation is that more solid components such as fats were present in the sample and hence, more than 20 minutes of centrifugation was  required. Desalted Sample: 60% ammonium sulfate is added to the crude extract that precipitates LDH proteins. The resulting 40% pellet theoretically contains most of the original LDH, which is re-suspended in very less volume (4ml) to create a more concentrated sample. This process leads to high concentration of salts in protein mixture that can interfere with subsequent purification steps. 4ml protein mixture underwent dialysis procedure that removes excess salts and our final volume after dialysis was 6ml. One possible explanation for increase in our volume could be that extraction buffer got mixed with protein mixture either due to tubing leaking or tubing clips not being properly tightened. Affinity Chromatography: Cibacron Blue column is an affinity column, which is specific to dehydrogenase type proteins, due to a compound structurally similar to NADH being attached covalently attached to the column. 13 fractions were collected and absorbance was measured at 280nm to check presence of LDH protein in the fractions. 1:10 dilution was performed if absorbance reading was above 1.5nm since it spectrophoretically indicates saturation and less than 1% light reaching the detector. During the addition of protein mixture (fraction# 4), high absorbance reading of 10nm was obtained (Fig.1). This could be due to lot of non-dehydrogenase-type proteins present in our sample that got eluted first during affinity chromatography. Second peak was seen after NAD+ was added since NAD solution results in the removal of the loosely bound protein. Third peak was seen after NADH was added since NADH solution results in release of maximum LDH proteins (Fig. 1). Enzyme Activity Assay: The LDH activity was measured spectrophotometrically by measuring the absorbance of NADH at 340 nm. Three peak fractions were selected for this assay based on their absorbance values obtained after adding NAD+ (fraction# 6, 7, 8) and other three after adding NADH in the affinity chromatography step (fraction# 10,11,12). A huge activity of 141umol/min/ml was seen at fraction# 7(PF1) which indicated that we had lot of proteins present in our sample. Second peak activity was seen at fraction #10 indicating that more LDH proteins is present in this fraction than in fraction# 11 (PF2) (fig.1). Based on this information, we selected fraction #10 as for our protein assay. Desalted showed highest activity among all the samples (Table1) possible due to errors occurring during dialysis explained previously. Figure 1. Absorbance readings of elutes obtained from affinity chromatography with LDH activity for 6 peak fractions. The desalted fraction was loaded to the Cibarcon blue column and proteins were eluted with Tris-PMSF, NAD+ and NADH wash subsequently. The absorbance at 280 nm of elutes were measured after each collected fractions. The LDH activity was calculated from the absorbance values obtained at 340nm. Protein Assay: We used BCA Pierce Assay to determine protein concentrations in our protein mixture. BSA standard curve was created for series of dilutions ranging from 0-2000  µg/ml and linear graph equation was used to calculate protein concentrations for the samples (Table 1). Based on Table 1, with each subsequent purification step, protein concentration decreases as sample become more concentrated with only LDH protein. Specific activity should increase and total activity should decrease with every purification step as samples get less and less diluted. Similar trend was observed in our study as well. However, exception is PF1 that has higher specific activity due to high activity suggesting more loosely bound proteins were eluted after NAD+ was added.

madonna and child Essay Example

madonna and child Essay Giovanni Bellini was born in 1426 1516. He was born in Venice, Italy. His father, Jacopo was also a painter. Giovanni more than likely began his career as an assistant in their fathers workshop. In hisfirst years as an artist Bellini was strongly influenced by his brother-in-law, Andrea Mantegna, from who he took a sculptures figure style. Giovanni Bellini was the founder of founder of the Venetian school of painting. He raised Venice to a centre of renaissance art that rivalled Florence and Rome. I will discuss two of his paintings further on in the essay. Madonna with the child (Greek Madonna) Madonna of the Meadow (Madonna del Prato) Madonna with the Child (Greek Madonna) 1460-64, Bellini Rafaello Santi was born in Urbane on good Friday 6th Aril 1483. His father was a painter and poet and worked for Frederica da Montefelto who was of the most famous princes and art patrons of the early Italian renaissance . Raphael helped his father in his studio from an early age. This is wh ere he is believed to have learned about art. His father died in 1494 and in 1504, Raphael moved to Florence and lived there for four years. He studied works by Leonardo da Vinci and Michelangelo here which inspired him even more. It was in Florence he began his series of Madonnas. I will talk about two of his Madonna paintings later. The Small Cowper Madonna Raphael c1505 In this essay I am going to discuss Raphaels and Bellinis approach to the theme Madonna and child. Both Bellini and Raphael painted many versions of the Madonna and child, both viewed this theme as a religious one however we can see that both portrayed the Madonna and child differently. Raphael painted Madonna and childs relationship as a warm and loving one. Be