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TABLE 2Amino acid requirement patterns relative to lysine = 100
More recent studies have examined the effects of glutamine and arginine in enhancing the immune system. Glutamine is preferentially metabolized by the intestinal mucosa and by lymphocytes. By maintaining mucosal cells it improves the gut barrier function against bacterial infection. As a precursor for glutathione (GSH) it helps maintain the antioxidant status of cells, especially the intestinal mucosa and lymphocytes. Inhibition of GSH synthesis leads to degeneration of mitochondria and structural damage to many tissues, including skeletal muscle and lung, but especially to fast turning over tissues such as intestinal mucosal cells (Mårtensson ., 1990). The GSH level in lymphocytes is very critical, decreasing with oxidative stress in a number of disease situations with loss of immunocompetence (Dröge and Breitkreutz, 2000; Grimble, 2001). The best studied case of GSH deficiency is human immunodeficiency virus (HIV). Not only is the extent of GSH depletion prognostic of the onset of AIDS, but supplementation with N-acetyl cysteine restores GSH levels and prevents progression of the disease (Herzenberg ., 1997). Giving whey protein isolate to HIV+ patients also increased GSH levels and improved body weight (Bounos ., 1993; Micke ., 2001). Whey protein isolate is particularly rich in methionine (2.5 g/16 g N) and cyst(e)ine (2.7 g/16 g N) and presumably acts to provide the necessary precursors for GSH synthesis. The importance of maintaining GSH levels is now being demonstrated in farm animals. Steers fed a diet supplying only 60 percent of maintenance requirement had liver GSH levels reduced to 26 percent of the control values (Sansinanea ., 2000). Protein deficient pigs had erythrocyte GSH reduced to 80 percent of the controls. An inflammatory stimulus further depleted GSH in the protein deficient pigs but was without effect in the protein replete pigs (Jahoor ., 1995). Nutritional strategies to increase GSH levels are not likely to be beneficial to the immune system in healthy animals but deserve investigation in cases where disease and oxidative stress are compromising the immune response and causing decreased GSH levels. For example, there is evidence of reduced immune response at the onset of lactation in high yielding cows, when body protein reserves are being rapidly mobilized to meet amino acids needs for milk protein secretion, and an increase in susceptibility to mastitis at this time (Piccinini ., 1999; Mehrzad ., 2001).
Figure 6. Feed efficiency ratio response to supplementing a lysine deficient diet with increments of lysine in male chicks from three to six weeks of age. The data are interpreted as either a) an exponential response over the whole range or b) a linear response to the requirement breakpoint. Source: Han and Baker, 1994
Microarray analysis using disiloxyl 70mer oligonucleotides
An arginine deficiency can be the cause of osteoporosis, especially in the case of older women, as proven in a study from 20025. An Italian study from 20036 showed that arginine in combination with other amino acids supported the growth of osteoblasts and also encouraged division. Experts therefore recommend that the administration of amino acids belong to all osteoporosis treatments, particularly as arginine works against bone destroying cells.7
They considered that
pycnogenol might bind to the blood vessel wall proteins and mucopolysaccharides and produce a capillary
'sealing' effect, leading to a reduced capillary permeability and oedema formation.
Defects in this transporter cause lysinuric protein intolerance.
Martinez, W.H., Frampton, V.L. & Cabell, C.A. 1961. Effects of gossypol and raffinose on lysine content and nutritive quality of proteins in meals from glandless cottonseed. , 9: 66-66.
Krogdahl, A., Bakke-McKellep, A.M., Røed, K.H. & Baeverfjord, G. 2000. Feeding Atlantic salmon L. soybean products: effects on disease resistance (furunculosis), and lysozyme and IgM levels in the intestinal mucosa. , 6: 77-84.
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Endogenous Synthesis of Arginine Plays an Important …
The role of endogenous nitric oxide (NO) synthesis was investigated in the regulation of the internal (ICA) and external carotid artery (ECA) beds of ventilated, anesthetized rats in a model in which the left common carotid artery was perfused from the aorta via an extracorporeal circuit under conditions of non-pulsatile controlled flow. The territories supplied by the extracranial ICA and ECA were studied separately following occlusion of the appropriate artery. An inhibitor of nitric oxide synthesis, NG-monomethyl-L-arginine (L-NMMA), and the NO synthase substrate L-arginine were administered via a jugular venous catheter. NO synthesis exerted an important influence on the pressure-flow relationships of the ICA and ECA circulations as L-NMMA increased input perfusion pressure at any given flow rate. However, in the presence of NO synthesis, hydraulic conductance increased rapidly with flow in the ICA, thereby stabilizing perfusion pressures over a wide range of flow rates, whereas this phenomenon was not evident in the ECA territory. Differences between the two circulations were further emphasized by observations that L-arginine antagonized the systemic hemodynamic response to L-NMMA and its effects on the conductance of the ECA bed, whereas the effects of L-NMMA were irreversible in the ICA territory.
Endogenous synthesis of arginine plays an important …
The amino acid is a crucial factor for bone creation as among other things, it supports the production of collagen. Collagen is a protein which is the basic component of various connective tissues (such as cartilage) and bone. In this way, arginine supports growth of the osteoblasts where bone mass is formed.4
An important role for endogenous synthesis of arginine …
Adequate energy must be supplied by the diet to make efficient use of dietary protein. The optimum energy density varies with species, digestive system, age and environment. In the ruminant, sufficient nitrogen and rumen degradable protein must be supplied to maximise bacterial fermentation, energy digestibility and feed intake. For young, fast growing animals and high yielding lactating animals, aim to feed high-energy diets to maximise production potential of animal protein. In older or less productive animals lower energy diets may be used to achieve maximum protein deposition or secretion without excess fat deposition. Include just sufficient protein with a good amino acid balance to support maximum protein deposition at the highest possible efficiency. Surplus protein may increase protein deposition through enhanced protein turnover, reduced efficiency of retention, greater N excretion and pollution, but with reduced net energy, less fat deposition and improved carcass composition. Protein requirements, expressed as a percentage of diet or as a protein-energy ratio, decline with age in growing animals. Phase feeding multiple diets with decreasing protein content reduces environmental pollution. Fish have lower energy requirements and require a greater protein: metabolizable energy (ME) ratio. For mammals and birds, express amino acid requirements and feed values as true ileal digestibility. For fish, faecal values suffice or can be estimated using faecal digestibility in mink or ileal digestibility in chicks. Choose protein supplements to provide amino acids that complement amino acids of basic (usually cereal) energy sources. In ruminants, the supplement should provide undegradable but intestinally digested amino acids to complement microbial protein. Methionine (or methionine + cystine) and lysine are first or second limiting. Protein requirements are reduced, with less pollution, by selecting proteins and amino acid supplements to approach the ideal protein pattern, but specifying maximum levels for excess amino acids will increase cost. Determine marginal response to amino acid supply to calculate target amino acid level in feed.
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