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In diagnosis, primary polydipsia is usually categorised as: Psychogenic (PPD) – caused by underlying psychiatric symptoms, including those caused by psychoses and rarely by affective disorders Non-psychogenic – another non-psychological cause, including idiopathic (unknown cause) The terms primary polydipsia and psychogenic polydipsia are sometimes incorrectly used interchangeably – to be considered psychogenic, the patient needs to have some other psychiatric symptoms, such as delusions involving fluid intake or other unusual behaviours. Primary polydipsia may have physiological causes, such as autoimmune hepatitis. Since primary polydipsia is a diagnosis of exclusion, the diagnosis may be made for patients who have medically unexplained excessive thirst, and this is sometimes incorrectly referred to as psychogenic rather than primary polydipsia.[13] Non-psychogenic Although primary polydipsia is usually categorised as psychogenic, there are some rare non-psychogenic causes. An example is polydipsia found in patients with autoimmune chronic hepatitis with severely elevated globulin levels.[41] Evidence for the thirst being non-psychogenic is gained from the fact that it disappears after treatment of the underlying disease.
Non-human animals Psychogenic polydipsia is also observed in some non-human patients, such as in rats and cats The globulins are a family of globular proteins that have higher molecular weights than albumins and are insoluble in pure water but dissolve in dilute salt solutions. Some globulins are produced in the liver, while others are made by the immune system. Globulins, albumins, and fibrinogen are the major blood proteins. The normal concentration of globulins in human blood is about 2.6-3.5 g/dL. The term "globulin" is sometimes used synonymously with "globular protein". However, albumins are also globular proteins, but are not globulins. All other serum globular proteins are globulins.

Contents 1 Types of globulins 2 Sizes ~ weights 3 Human blood plasma levels 4 Nonhuman globulins 5 Pseudoglobulins and euglobulins 6 References 7 External links Types of globulins Schematic representation of a protein electrophoresis gel All globulins fall into one of the following four categories : Alpha 1 globulins Alpha 2 globulins Beta globulins Gamma globulins (one group of gamma globulins is the immunoglobulins, which are also known as "antibodies") Globulins can be distinguished from one another using serum protein electrophoresis. Globulins exert oncotic pressure. Their deficiency results in loss of carrier functions of globulins, oedema due to decreased oncotic pressure, and susceptibility to infections due to decreased gamma-globulins (immuno-globulins) leading to decreased production of antibodies. Sizes ~ weights Globulins exist in various sizes. The lightest globulins are the alpha globulins, which typically have molecular weights of around 93 kDa, while the heaviest class of globulins are the gamma globulins, which typically weigh about 1193 kDa. Being the heaviest, the gamma globulins are among the slowest to segregate in gel electrophoresis. The immunologically active gamma globulins are also called "immunoglobulins" or "antibodies". Human blood plasma levels The normal concentration of globulins in human blood is about 2.6-4.6 g/dL. Reference ranges for blood tests, comparing blood content of globulins (shown in purple at right) with other constituents. Nonhuman globulins Crystal structure of a pumpkin seed globulin Globulin proteins exist not only in other animal species, but also in plants. Vicilin and legumin, from peas and other legumes, function as protein storage within seeds. These proteins can cause allergic reactions if they bind with human IgE antibodies.[1] Pseudoglobulins and euglobulins Pseudoglobulins are a class of globulins that are more soluble in ammonium sulfate than euglobulins. Pseudoglobulins are also soluble in pure water, while euglobulins are not Ammonium sulfate (American English and international scientific usage; ammonium sulphate in British English); (NH4)2SO4, is an inorganic salt with a number of commercial uses. The most common use is as a soil fertilizer. It contains 21% nitrogen and 24% sulfur. Contents 1 Uses 1.1 Laboratory use 1.2 Food additive 1.3 Other uses 2 Preparation 3 Properties 4 Reactions 5 Legislation and control 6 See also 7 References 8 Further reading 9 External links Uses The primary use of ammonium sulfate is as a fertilizer for alkaline soils. In the soil the ammonium ion is released and forms a small amount of acid, lowering the pH balance of the soil, while contributing essential nitrogen for plant growth. The main disadvantage to the use of ammonium sulfate is its low nitrogen content relative to ammonium nitrate, which elevates transportation costs.[2] It is also used as an agricultural spray adjuvant for water-soluble insecticides, herbicides, and fungicides. There, it functions to bind iron and calcium cations that are present in both well water and plant cells. It is particularly effective as an adjuvant for 2,4-D (amine), glyphosate, and glufosinate herbicides. Laboratory use Ammonium sulfate precipitation is a common method for protein purification by precipitation. As the ionic strength of a solution increases, the solubility of proteins in that solution decreases. Ammonium sulfate is extremely soluble in water due to its ionic nature, therefore it can "salt out" proteins by precipitation.[3] Due to the high dielectric constant of water, the dissociated salt ions being cationic ammonium and anionic sulfate are readily solvated within hydration shells of water molecules. The significance of this substance in the purification of compounds stems from its ability to become more so hydrated compared to relatively more nonpolar molecules and so the desirable non-polar molecules coalesce and precipitate out of the solution in a concentrated form. This method is called salting out and necessitates the use of high salt concentrations that can reliably dissolve in the aqueous mixture. The percentage of the salt used is in comparison to the maximal concentration of the salt in the mixture can dissolve. As such, although high concentrations are needed for the method to work adding an abundance of the salt, over 100%, can also oversaturate the solution, therefore, contaminating the non-polar precipitate with salt precipitate.[4] A high salt concentration, which can be achieved by adding or increasing the concentration of ammonium sulfate in a solution, enables protein separation based on a decrease in protein solubility; this separation may be achieved by centrifugation. Precipitation by ammonium sulfate is a result of a reduction in solubility rather than protein denaturation, thus the precipitated protein can be solubilized through the use of standard buffers.[5] Ammonium sulfate precipitation provides a convenient and simple means to fractionate complex protein mixtures.[6] In the analysis of rubber lattices, volatile fatty acids are analyzed by precipitating rubber with a 35% ammonium sulfate solution, which leaves a clear liquid from which volatile fatty acids are regenerated with sulfuric acid and then distilled with steam. Selective precipitation with ammonium sulfate, opposite to the usual precipitation technique which uses acetic acid, does not interfere with the determination of volatile fatty acids.[7] Food additive As a food additive, ammonium sulfate is considered generally recognized as safe (GRAS) by the U.S. Food and Drug Administration,[8] and in the European Union it is designated by the E number E517. It is used as an acidity regulator in flours and breads.[9][10][11] Other uses In the treatment of drinking water, ammonium sulfate is used in combination with chlorine to generate monochloramine for disinfection.[12] Ammonium sulfate is used on a small scale in the preparation of other ammonium salts, especially ammonium persulfate. Ammonium sulfate is listed as an ingredient for many United States vaccines per the Center for Disease Control.[13] A saturated solution of ammonium sulfate in heavy water (D2O) is used as an external standard in sulfur (33S) NMR spectroscopy with shift value of 0 ppm. Ammonium sulfate has also been used in flame retardant compositions acting much like diammonium phosphate. As a flame retardant, it increases the combustion temperature of the material, decreases maximum weight loss rates, and causes an increase in the production of residue or char.[14] Its flame retardant efficacy can be enhanced by blending it with ammonium sulfamate.[citation needed] It has been used in aerial firefighting. Ammonium sulfate has been used as a wood preservative, but due to its hygroscopic nature, this use has been largely discontinued because of associated problems with metal fastener corrosion, dimensional instability, and finish failures. Preparation Ammonium sulfate is made by treating ammonia, often as a by-product from coke ovens, with sulfuric acid: 2 NH3 + H2SO4 ? (NH4)2SO4 A mixture of ammonia gas and water vapor is introduced into a reactor that contains a saturated solution of ammonium sulfate and about 2 to 4% of free sulfuric acid at 60 °C. Concentrated sulfuric acid is added to keep the solution acidic, and to retain its level of free acid. The heat of reaction keeps reactor temperature at 60 °C. Dry, powdered ammonium sulfate may be formed by spraying sulfuric acid into a reaction chamber filled with ammonia gas. The heat of reaction evaporates all water present in the system, forming a powdery salt. Approximately 6000M tons were produced in 1981.[2] Ammonium sulfate also is manufactured from gypsum (CaSO4·2H2O). Finely divided gypsum is added to an ammonium carbonate solution. Calcium carbonate precipitates as a solid, leaving ammonium sulfate in the solution. (NH4)2CO3 + CaSO4 ? (NH4)2SO4 + CaCO3 Ammonium sulfate occurs naturally as the rare mineral mascagnite in volcanic fumaroles and due to coal fires on some dumps.[15] Properties Ammonium sulfate becomes ferroelectric at temperatures below -49.5 °C. At room temperature it crystallises in the orthorhombic system, with cell sizes of a = 7.729 Å, b = 10.560 Å, c = 5.951 Å. When chilled into the ferrorelectric state, the symmetry of the crystal changes to space group Pna21

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