Hy-fy Hitch- Zygomatico-hyoid Suspension for Dysphagia

Hy-fy Hitch- Zygomatico-hyoid Suspension for Dysphagia Hy-fy Hitch- Zygomatico-hyoid Suspension for the Managment of Post Surgical Dysphagia abstract: Dysphagia is not only a main symptom of the head and neck cancer but also the dangerous complication of the various surgical and other treatment modalities for the same. Though various studies have been done to diagnose this condition but very little is done towards the surgical management of this life threatening condition. through this article the new surgical technique of managing oroesophgeal dysphagia by hyoid suspension. Our technique zygomatico-hyoid suspension is simple and logically effective way of managing dysphagia secondary to the surgical resection of lesion in the patient with head and neck cancer. Though this technique is not tried in large number of patients hence the long term benefits and overall improvement in patients quality of life is yet to be ascertained but still it can be a new direction in the surgical mangament of dysphagia. Introduction Dysphagia is a term derived from the Greek words dys (difficulty) and phagein (to eat)1. It is a symptom that expresses a disorder in the transport of food and endogenous secretions (saliva) through the upper digestive tract. Oropharyngeal dysphagia (OD) is a more anatomically restricted term referred to alterations in the transfer of the bolus from the mouth to the esophagus (that means, in bolus propelling from the mouth to the pharynx, in the pharyngeal reconfiguration during the swallow, or in the opening of the upper esophageal sphincter.2 OD is an inescapable concern in the management of patients with oral cancer. Being as a symptom at presentation, as an adverse effect during whatever the treatment, or as sequelae compromising the quality of life of the patients, swallowing disorders have to be adequately anticipated and dealt with. For an outcome to be considered functional, the patient has to be able to swallow in an effective and safe manner. Actually, preserving a functional deglutition is usually the most important goal of the different function-preserving surgical techniques in head and neck cancer surgery. Normal oropharyngeal swallowing: swallowing is mainly divided into three phases: 1) preparatory oral phase ,2) oral phase and the last 3) pharyngeal and oesophageal phase. mechanically ,several closely coordinated actions are involved:(1) elevation and retraction of the soft palate with closure of oropharynx,(2) UES opening, (3) laryngeal closure at the level of the laryngeal vestibule,(4) tongue loading (ramping), (5) tongue pulsion ,and (6) pharyngeal clearance. a fundamental aspect of deglutitive pharyngeal reconfiguration is in transforming the oropharynx from a respiratory to a swallowing pathway by opening the inlet to the esophagus and sealing the inlet to the larynx. Laryngeal vestibule closure and hence airway protection during swallowing is achieved by laryngeal elevation and anterior tilting of the arytenoid cartilages against the base of the epiglottis. UES opening results from anterior traction caused by contraction of the suprahyoid and infrahyoid musculature evident fluoroscopically by anterior hyoid movement. Pathophysiology of dysphagia: Can be divided into two categories: 1) directly due to the resection of the tissues involved in the swallowing i.e.tongue . 2) due to the damage caused by the radiation therapy by following ways: a: decreased pharyngeal peristalsis. b: decresed or defective posterior inversion of the base of the tongue towards the posterior pharyngeal wall. c: decreased elevation of hyoid bone and larynx and decreased inversion of epiglottis. The use of laryngeal suspension as a technique to improve function following surgcial resection of the anterior floor of the mouth was 1st decribed by edgerton and duncan and DesPrez and Kiehn.3,4 later Jabaley and Hoopes simplified the concept of laryngeal suspension after partial or complete resection of hyomandibular complex by means of a heavy chromic catgut suture between the thyroid cartilage and mandibular symphysis on the premise that the main vector of force required to support the larynx is anterior and superior in the midline.5 Goode R.L. also described the similar technique of laryngeal suspension after total laryngectomy by thyroid mandibular suspension and he found that swallowing function was improved significantly with his method of laryngeal suspension.6 Hillel A.D. and Goode R.L. gave lateral laryngeal suspension technique in which the throid cartlage was suspended to the condyle of resected mandible a modification of Goode R.L`s original technique, the advantage of this technique is it causes superior as well as lateral movement movement of larynx which widens the opening of opposite hypopharynx.7 al these techniques have proven that the hyoid suspension does improve swallowing function to some extent but all these techniques are hyomandibular suspension and our techniques is the only technique in which we have used zygomatic bone a support bone through which hyoid is suspended and in our view this technique provieds the most stable and most effective way of displacing hyoid anterio-superiorly resulting in the better swallowing control.in this article we describe our method of hyoid-zygomtic suspension. Material and methods: We perform zygomatico-hyoid suspension in all the patients undergoing total or partial glossectomy with or without mandible resection .the procedure was performed at the mahatma gandhi cnacer institute miraj . Notes on Hyoid-zygomatic Suspension Technique The hyoid suspension in which 24 gauge stainless steel wire was prestreched and using a awl 26cm in length a circumzygomatic to the hyoid bone suspension was carried out by the Key steps were the following. the procedure was performed under genearal anesthesia while doing primary resection of the tumor .patient was placd in anti-trendelenburg position with neck hyperextension. Incision was given in natural skin crease between the hyoid inferior body and the thyroid notch. Median strap muscle dissection between two imaginary parasagittal planes crossing the lesser cornu of the hyoid bone was carried out. Hyoid bone mobilizing test in anterosuperior direction carried out permanent hyoid fixation after having tested the correct position of the thyroid cartilage below the hyoid bone, following fixed steps which are as follows:The zygomatic arch is palpated and puncture wound is performed at the origin of the temporal process of the zygomatic bone.Two pre-streched 24 gauge wires are passe d circumferentially around the hyoid bone in the region where the insertion of the fibrous loop for the intermediate diagastric tendon is present.Later awl is inserted from the arch puncture wound and passed anterior to the masseteric muscle and brought to the hyoid bone body region where the already wire loops are present.The wire is fed into the eye of the awl and later pulled out.This wire is removed from the awls eye and stablised.The awl now is reinserted superficial to the arch brought out from the previous anterior massetric site to the hyoid bone, the other end of wire is fed in the eye and the wire along with the awl is brought out.Traction is given bilaterally and the mobility of the hyoid along with its infrahyoid component is examined.Mandibular movements have to be checked before the wires are twisted and stabilised.Untoward traction is to be avoided in order to avoid hyoid bone fractures.Incision lines are closed in layers. Postoperative Followup Postoperatively all patients tolerated the procedure well, with no intra- or postoperative complications. patients .all patients were kept on nasogatric tube ( NGT ) feeding for minimum 3 weeks postoperative period after which the decision to remove the tube and oral feeding was taken on the basis of patient to patient ability to swallow . No special or additional post-operative care or assessment is required . Discussion The hyoid is a u-shaped bone located in the anterior neck midline, at the centre of three force vectors directed, respectively, towards the mandible, sternum, and mastoid process. It gives insertion to the middle constrictor muscles, which form the lateral wall of the hypopharynx. The suspension of this bone to the Zygomatic bone restores the inferior collapse of the reconstructed floor and lateral mandibular region and improve the tone of the middle constrictor muscles. this technique unlike all the previous technique doesnt take support of the mandible at all hence in cases where in mandible resection is performed along with the tongue or the larynx this technique is probably the only option available to the surgeon to suspend the hyoid bone. Without resuspension, it is speculated that resection of submental lateral mandibular region may lead to inferior and posterior displacement of the hyoid bone. A posterior displacementof the hyoid bone may be implicated in obstruction of the p haryngeal airway which in turn may lead to Dysphagia, or swallowing impairment . The postsurgical alteration in size and position of the hard and soft tissues surrounding the pharyngeal space is also responsible for the airway obstruction. CONCLUSION: Cicumzygomatic hyoid suspension technique is a innovative technique and it is the only technique of hyoid suspension in which instead of mandible the support is taken from zygomatic bone . as in this technique the vector is in same direction but its supporting bone absolutely nonmobile there by giving greater elevation and stable anterior displacement in comparison to the other tehcniques of hyoid suspension. we found that swallowing and infra hyoid functions improvedin our patient thereby QOL improved. This Hyoid suspension technique is effective when short-term results are considered. The necessity of a more valuable anatomic-based diagnostic approach is crucial to guide the patient selection. Long-term follow-ups and randomized prospective trials with case-control series are needed to increase the level of evidence of this surgery.

Comparing the Innocent Criminal in Black Boy, Uncle Toms Children, Nat

The Innocent Criminal in Black Boy, Uncle Tom's Children, Native Son, and The Outsider      Ã‚   "It is probably a mere accident that I never killed," Richard Wright commented offhandedly in an interview with Robert Moss (596).   After reading several of Wright's works, one can easily understand what Wright means by this statement.   In his books Black Boy, Uncle Tom's Children, Native Son, and The Outsider, Wright suggests that white society has transformed black people into criminals.   The source of this claim comes from Wright's personal experiences as a Negro in the Deep South.   Whether pushed to crime from necessity or for personal fulfillment and self-realization, the protagonists of Wright's works are innocent criminals; they know that the ultimate crime for which they are being punished is the crime of being black.   Circumstances created by a racist social order place the characters in intolerable positions that coerce them into villainous activities.      Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚   In his autobiographical novel, Black Boy, Wright supports this theory using himself as an example.   In the tradition of the slave autobiography, Black Boy provides details of Wright's life from early childhood to his arrival in Chicago.   As Joyce Ann Joyce says, Black Boy:      Ã‚  Ã‚   ...is a realistic and poetic account of the hunger Wright endured as a child, his  Ã‚  Ã‚  Ã‚   closeness to his mother, the effect of his mother's illness, his problems with his father, his father's desertion, the violence he experienced from his mother's relatives, his love of words and books, his discovery of racism and his developing racial consciousness, his fight against his mother's and grandmother's religion, his scanty education, ... and the development of his individuality... ...chard Wright.   New York: Harcourt, 1969.   Rpt. in   Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚   Richard Wright's Native Son: Modern Critical Interpretations.   New York: Chelsea House, 1988. Moss, Robert F.   "Caged Misery."   Saturday Review.   Jan. 21, 1978, 45-7.   Rpt. in Contemporary Literary Criticism. Vol. 14.   Detroit: Gale, 1980. Skerrett, Joseph T., Jr.   "Composing Bigger: Wright and the Making of Native Son." in Richard Wright's   Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚   Native Son:   Modern Critical Interpretations.   New York: Chelsea House, 1988. Wright, Richard.   Black Boy.   New York: Harper, 1944. _____.   "How Bigger Was Born."   Saturday Review.   June 1, 1940, n.pag.   Rpt. in Native Son.   New   Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚  Ã‚   York: Harper, 1940. _____.   Native Son.   New York: Harper, 1940. _____.   The Outsider.   New York: Harper, 1953. _____.   Uncle Tom's Children.   New York: Harper, 1936.

Glutathione

Glutathione (GSH) is a tripeptide that contains an unusual peptide linkage between the amine group of cysteine (which is attached by normal peptide linkage to a glycine) and the carboxyl group of the glutamate side-chain. It is an antioxidant, preventing damage to important cellular components caused by reactive oxygen species such as free radicals and peroxides. [2] Thiol groups are reducing agents, existing at a concentration of approximately 5 mM in animal cells. Glutathione reduces disulfide bonds formed within cytoplasmic proteins to cysteines by serving as an electron donor. In the process, glutathione is converted to its oxidized form glutathione disulfide (GSSG), also called L(-)-Glutathione. Glutathione is found almost exclusively in its reduced form, since the enzyme that reverts it from its oxidized form, glutathione reductase, is constitutively active and inducible upon oxidative stress. In fact, the ratio of reduced glutathione to oxidized glutathione within cells is often used as a measure of cellular toxicity. 3] Glutathione is not an essential nutrient (meaning it does not have to be obtained via food), since it can be synthesized in the body from the amino acids L-cysteine, L-glutamic acid, and glycine. The sulfhydryl (thiol) group (SH) of cysteine serves as a proton donor and is responsible for the biological activity of glutathione. Provision of this amino acid is the rate-limiting factor in glutathione synthesis by the cells, since cysteine is relatively rare in foodstuffs. Furthermore, if released as the free amino acid, cysteine is toxic and spontaneously catabolized in the gastrointestinal tract and blood plasma. [4] Glutathione is synthesized in two adenosine triphosphate-dependent steps: * First, gamma-glutamylcysteine is synthesized from L-glutamate and cysteine via the enzyme gamma-glutamylcysteine synthetase (a. k. a. glutamate cysteine ligase, GCL). This reaction is the rate-limiting step in glutathione synthesis. citation needed] * Second, glycine is added to the C-terminal of gamma-glutamylcysteine via the enzyme glutathione synthetase. Animal glutamate cysteine ligase (GCL) is a heterodimeric enzyme composed of a catalytic (GCLC) and modulatory (GCLM) subunit. GCLC constitutes all the enzymatic activity, whereas GCLM increases the catalytic efficiency of GCLC. Mice lacking GCLC (i. e. , all de novo GSH synthesis) die before birth. [5] Mice lacking GCLM demonstrate no outward phenotype, but exhibit marked decrease in GSH and increased sensiti vity to toxic insults. 6][7][8] While all cells in the human body are capable of synthesizing glutathione, liver glutathione synthesis has been shown to be essential. Mice with genetically-induced loss of GCLC (i. e. , GSH synthesis) only in the liver die within 1 month of birth. [9] The plant glutamate cysteine ligase (GCL) is a redox-sensitive homodimeric enzyme, conserved in the plant kingdom. [10] In an oxidizing environment, intermolecular disulfide bridges are formed and the enzyme switches to the dimeric active state. The mid-point potential of the critical cysteine pair is -318 mV. In addition to the redox-dependent control is the plant GCL enzyme feedback inhibited by GSH. [11] GCL is exclusively located in plastids, and glutathione synthetase is dual-targeted to plastids and cytosol, thus are GSH and gamma-glutamylcysteine exported from the plastids. [12] Both glutathione biosynthesis enzymes are essential in plants; knock-outs of GCL and GS are lethal to embryo and seedling. [13] The biosynthesis pathway for glutathione is found in some bacteria, like cyanobacteria and proteobacteria, but is missing in many other bacteria. Most eukaryotes synthesize glutathione, including humans, but some do not, such as Leguminosae, Entamoeba, and Giardia. The only archaea that make glutathione are halobacteria. [14][15] [edit] Function Glutathione exists in reduced (GSH) and oxidized (GSSG) states. In the reduced state, the thiol group of cysteine is able to donate a reducing equivalent (H++ e-) to other unstable molecules, such as reactive oxygen species. In donating an electron, glutathione itself becomes reactive, but readily reacts with another reactive glutathione to form glutathione isulfide (GSSG). Such a reaction is possible due to the relatively high concentration of glutathione in cells (up to 5 mM in the liver). GSH can be regenerated from GSSG by the enzyme glutathione reductase. In healthy cells and tissue, more than 90% of the total glutathione pool is in the reduced form (GSH) and less than 10% exists in the disulfide form (GSSG). An increased GSSG-to-GSH ratio is considered indicative of oxidative str ess. Glutathione has multiple functions: It is the major endogenous antioxidant produced by the cells, participating directly in the neutralization of free radicals and reactive oxygen compounds, as well as maintaining exogenous antioxidants such as vitamins C and E in their reduced (active) forms. [16][citation needed] * Regulation of the nitric oxide cycle, which is critical for life but can be problematic if unregulated [17] * Through direct conjugation, it detoxifies many xenobiotics (foreign compounds) and carcinogens, both organic and inorganic. This includes heavy metals such as mercury, lead, and arsenic. [citation needed] * It is essential for the immune system to exert its full potential, e. g. , (1) modulating antigen presentation to lymphocytes, thereby influencing cytokine production and type of response (cellular or humoral) that develops, (2) enhancing proliferation of lymphocytes, thereby increasing magnitude of response, (3) enhancing killing activity of cytotoxic T cells and NK cells, and (4) regulating apoptosis, thereby maintaining control of the immune response. citation needed] * It plays a fundamental role in numerous metabolic and biochemical reactions such as DNA synthesis and repair, protein synthesis, prostaglandin synthesis, amino acid transport, and enzyme activation. Thus, every system in the body can be affected by the state of the glutathione system, especially the immune system, the nervous system, the gastrointestinal system and the lungs. [4] Function in animals GSH is known as a substrate in both conjugation reactions and reduction reactions, catalyzed by glutathione S-transferase enzymes in cytosol, microsomes, and mitochondria. However, it is also capable of participating in non-enzymatic conjugation with some chemicals. In the case of N-acetyl-p-benzoquinone imine (NAPQI), the reactive cytochrome P450-reactive metabolite formed by paracetamol (or acetaminophen as it is known in the US), that becomes toxic when GSH is depleted by an overdose of acetaminophen, Glutathione is an essential antidote to overdose. Glutathione conjugates to NAPQI and helps to detoxify it. In this capacity, it protects cellular protein thiol groups, which would otherwise become covalently modified; when all GSH has been spent, NAPQI begins to react with the cellular proteins, killing the cells in the process. The preferred treatment for an overdose of this painkiller is the administration (usually in atomized form) of N-acetyl-L-cysteine (often as a trademarked preparation called Mucomyst ® [1]), which is processed by cells to L-cysteine and used in the de novo synthesis of GSH. Glutathione (GSH) participates in leukotriene synthesis and is a cofactor for the enzyme glutathione peroxidase. It is also important as a hydrophilic molecule that is added to lipophilic toxins and waste in the liver during biotransformation before they can become part of the bile. Glutathione is also needed for the detoxification of methylglyoxal, a toxin produced as a by-product of metabolism. This detoxification reaction is carried out by the glyoxalase system. Glyoxalase I (EC 4. 4. 1. ) catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-lactoyl-glutathione. Glyoxalase II (EC 3. 1. 2. 6) catalyzes the hydrolysis of S-D-lactoyl-glutathione to glutathione and D-lactic acid. Glutathione has recently been used as an inhibitor of melanin in the cosmetics industry. In countries like Japan and the Philippines, this product is sold as a whitening soap. Glutathione competitively inhibits melanin synthesis in the reaction of tyrosinase and L-DOPA by interrupting L-DO PA's ability to bind to tyrosinase during melanin synthesis. The inhibition of melanin synthesis was reversed by increasing the concentration of L-DOPA, but not by increasing tyrosinase. Although the synthesized melanin was aggregated within 1 h, the aggregation was inhibited by the addition of glutathione. These results indicate that glutathione inhibits the synthesis and agglutination of melanin by interrupting the function of L-DOPA. â€Å"[18] Function in plants In plants, glutathione is crucial for biotic and abiotic stress management. It is a pivotal component of the glutathione-ascorbate cycle, a system that reduces poisonous hydrogen peroxide. 19] It is the precursor of phytochelatins, glutathione oligomeres that chelate heavy metals such as cadmium. [20] Glutathione is required for efficient defence against plant pathogens such as Pseudomonas syringae and Phytophthora brassicae. [21] APS reductase, an enzyme of the sulfur assimilation pathway uses glutathione as electron donor. Other enzymes using glutathione as substrate are glutare doxin, these small oxidoreductases are involved in flower development, salicylic acid and plant defence signalling. [22] [edit] Supplementation Raising GSH levels through direct supplementation of glutathione is difficult. Research suggests that glutathione taken orally is not well absorbed across the gastrointestinal tract. In a study of acute oral administration of a very large dose (3 grams) of oral glutathione, Witschi and coworkers found â€Å"it is not possible to increase circulating glutathione to a clinically beneficial extent by the oral administration of a single dose of 3 g of glutathione. â€Å"[23][24] Vitamin D increases glutathione levels in the brain and appears to be a catalyst for glutathione production. 25] The amount of activated vitamin D in the brain is tied to how much vitamin D3 one has, either ingested through supplements or created in the skin via sun exposure. This suggests taking vitamin D3 supplements and/or getting adequate sun exposure boosts glutathione production. In addition, plasma and liver GSH concentrations can be raised by administration of certain supplements that serve as GSH precu rsors. N-acetylcysteine, commonly referred to as NAC, is the most bioavailable precursor of glutathione. 26] Other supplements, including S-adenosylmethionine (SAMe)[27][28][29] and whey protein[30][31][32][33][34][35] have also been shown to increase glutathione content within the cell. NAC is available both as a drug and as a generic supplement. Alpha lipoic acid has also been shown to restore intracellular glutathione. [36][37] Melatonin has been shown to stimulate a related enzyme, glutathione peroxidase,[38] and silymarin, an extract of the seeds of the milk thistle plant (Silybum marianum) has also demonstrated an ability to replenish glutathione levels. [39][40] Glutathione is a tightly regulated intracellular constituent, and is limited in its production by negative feedback inhibition of its own synthesis through the enzyme gamma-glutamylcysteine synthetase, thus greatly minimizing any possibility of over dosage. Glutathione augmentation using precursors of glutathione synthesis or intravenous glutathione is a strategy developed to address states of glutathione deficiency, high oxidative stress, immune deficiency, and xenobiotic overload in which glutathione plays a part in the detoxification of the xenobiotic in question (especially through the hepatic route). Glutathione deficiency states include, but are not limited to, HIV/AIDS, chemical and infectious hepatitis, myalgic encephalomyelitis chronic fatigue syndrome ME / CFS,[41][42][43] prostate and other cancers, cataracts, Alzheimer's disease, Parkinson's disease, chronic obstructive pulmonary disease, asthma, radiation poisoning, malnutritive states, arduous physical stress, and aging, and has been associated with suboptimal immune response. Many clinical pathologies are associated with oxidative stress and are elaborated upon in numerous medical references. [4][44][45] Low glutathione is also strongly implicated in wasting and negative nitrogen balance,[46] as seen in cancer, AIDS, sepsis, trauma, burns and even athletic overtraining. Glutathione supplementation can oppose this process, and in AIDS, for example, result in improved survival rates. [47] However, studies in many of these conditions have not been able to differentiate between low glutathione as a result of acutely (as in septic patients) or chronically (as in HIV) increased oxidative stress, and increased pathology as a result of preexisting deficiencies. Schizophrenia and bipolar disorder are associated with lowered glutathione. Accruing data suggest that oxidative stress may be a factor underlying the pathophysiology of bipolar disorder (BD), major depressive disorder (MDD), and schizophrenia (SCZ). Glutathione (GSH) is the major free radical scavenger in the brain. [48] Diminished GSH levels elevate cellular vulnerability towards oxidative stress; characterized by accumulating reactive oxygen species. Replenishment of glutathione using N-acetyl cysteine has been shown to reduce symptoms of both disorders. citation needed] Cancer Preliminary results indicate glutathione changes the level of reactive oxygen species in isolated cells grown in a laboratory,[49][50] which may reduce cancer development. [51] [52] None of these tests were performed in humans. However, once a cancer has already developed, by conferring resistance to a number of chemotherapeutic drugs, elevated levels of glutathione in tumor cells are able to protect cancer ous cells in bone marrow, breast, colon, larynx, and lung cancers. 53] [edit] Pathology Excess glutamate at synapses, which may be released in conditions such as traumatic brain injury, can prevent the uptake of cysteine, a necessary building-block of glutathione. Without the protection from oxidative injury afforded by glutathione, cells may be damaged or killed. [54] Methods to determine glutathione Reduced glutathione may be visualized using Ellman's reagent or bimane derivates such as monobromobimane. The monobromobimane method is more sensitive. In this procedure, cells are lysed and thiols extracted using a HCl buffer. The thiols are then reduced with dithiothreitol (DTT) and labelled by monobromobimane. Monobromobimane becomes fluorescent after binding to GSH. The thiols are then separated by HPLC and the fluorescence quantified with a fluorescence detector. Bimane may also be used to quantify glutathione in vivo. The quantification is done by confocal laser scanning microscopy after application of the dye to living cells. 55] Another approach, which allows to measure the glutathione redox potential at a high spatial and temporal resolution in living cells is based on redox imaging using the redox-sensitive green fluorescent protein (roGFP)[56] or redox sensitive yellow fluorescent protein. . When we speak of glutathione, what will really come to mind is that glutathione which most Filipino thought of as a whitening agent. It comes in soaps and any other beauty products which hopefully will make one whiter and fairer when used. But what we really don’t know is that glutathione is found in each of three trillion cells in our body. It is the most powerful an antioxidant which we cannot find in a fruit or in a berry a common but it is found in our body. In fact its absence will make one die. In my first blog I ‘ve told you about the glutathione story. Now I’m going to tell you what glutathione really is and its role to our over all well being. So what is glutathione really: Glutathione is a tripeptide, What is glutathione?

A Researcher Skilled In Reading, Evaluating, Conducting and Reporting Research Free Essay Example, 3250 words

The abstract briefly describes what the researchers did and the results of the study. The abstract gives a better understanding of what has been done which gives the reader an understanding of the relevance of the study. The introduction gives an outline of the problem or issue being studied, summarizes any existing research that was done before the current study, gives the research question and/or the objectives and the hypotheses. The method section describes techniques that were used to conduct the study. In this section, the reader will find information on the design, sample, environment that was used and the data collection method and the analysis of the research. The qualitative method provides information about the experiences that people have in many situations. In healthcare, this research can show how patients feel and it can provide information about other cultures, genders, and on special populations like immigrants or those with a specific disease like HIV/AIDS (Davies and Logan, 2008). Qualitative research is the area in which most survey research will be defined although there are times when it can be used in quantitative research. We will write a custom essay sample on A Researcher Skilled In Reading, Evaluating, Conducting and Reporting Research or any topic specifically for you Only $17.96 $11.86/page