Solubility is the property of a solid, liquid or gaseous chemical substance called solute to dissolve in a solid, liquid or gaseous solvent. The solubility of a substance fundamentally depends on the physical and chemical properties of the solute and solvent as well as on temperature and presence of other chemicals of the solution; the extent of the solubility of a substance in a specific solvent is measured as the saturation concentration, where adding more solute does not increase the concentration of the solution and begins to precipitate the excess amount of solute. Insolubility is the inability to dissolve in a liquid or gaseous solvent. Most the solvent is a liquid, which can be a pure substance or a mixture. One may speak of solid solution, but of solution in a gas. Under certain conditions, the equilibrium solubility can be exceeded to give a so-called supersaturated solution, metastable. Metastability of crystals can lead to apparent differences in the amount of a chemical that dissolves depending on its crystalline form or particle size.
A supersaturated solution crystallises when'seed' crystals are introduced and rapid equilibration occurs. Phenylsalicylate is one such simple observable substance when melted and cooled below its fusion point. Solubility is not to be confused with the ability to'dissolve' a substance, because the solution might occur because of a chemical reaction. For example, zinc'dissolves' in hydrochloric acid as a result of a chemical reaction releasing hydrogen gas in a displacement reaction; the zinc ions are soluble in the acid. The solubility of a substance is an different property from the rate of solution, how fast it dissolves; the smaller a particle is, the faster it dissolves although there are many factors to add to this generalization. Crucially solubility applies to all areas of chemistry, inorganic, physical and biochemistry. In all cases it will depend on the physical conditions and the enthalpy and entropy directly relating to the solvents and solutes concerned. By far the most common solvent in chemistry is water, a solvent for most ionic compounds as well as a wide range of organic substances.
This is a crucial factor in much environmental and geochemical work. According to the IUPAC definition, solubility is the analytical composition of a saturated solution expressed as a proportion of a designated solute in a designated solvent. Solubility may be stated in various units of concentration such as molarity, mole fraction, mole ratio, mass per volume and other units; the extent of solubility ranges from infinitely soluble such as ethanol in water, to poorly soluble, such as silver chloride in water. The term insoluble is applied to poorly or poorly soluble compounds. A number of other descriptive terms are used to qualify the extent of solubility for a given application. For example, U. S. Pharmacopoeia gives the following terms: The thresholds to describe something as insoluble, or similar terms, may depend on the application. For example, one source states that substances are described as "insoluble" when their solubility is less than 0.1 g per 100 mL of solvent. Solubility occurs under dynamic equilibrium, which means that solubility results from the simultaneous and opposing processes of dissolution and phase joining.
The solubility equilibrium occurs. The term solubility is used in some fields where the solute is altered by solvolysis. For example, many metals and their oxides are said to be "soluble in hydrochloric acid", although in fact the aqueous acid irreversibly degrades the solid to give soluble products, it is true that most ionic solids are dissolved by polar solvents, but such processes are reversible. In those cases where the solute is not recovered upon evaporation of the solvent, the process is referred to as solvolysis; the thermodynamic concept of solubility does not apply straightforwardly to solvolysis. When a solute dissolves, it may form several species in the solution. For example, an aqueous suspension of ferrous hydroxide, Fe2, will contain the series + as well as other species. Furthermore, the solubility of ferrous hydroxide and the composition of its soluble components depend on pH. In general, solubility in the solvent phase can be given only for a specific solute, thermodynamically stable, the value of the solubility will include all the species in the solution.
Solubility is defined for specific phases. For example, the solubility of aragonite and calcite in water are expected to differ though they are both polymorphs of calcium carbonate and have the same chemical formula; the solubility of one substance in another is determined by the balance of intermolecular forces between the solvent and solute, the entropy change that accompanies the solvation. Factors such as temperature and pressure will alter this balance. Solubility may strongly depend on the presence of other species dissolved in the solvent, for example, complex-forming anions in liquids. Solubility will depend on the excess or deficiency of a common ion in the solution, a phenomenon known as the common-ion effect. To a lesser extent, solubility will depend on the ionic strength of solutions; the last two effects can be quantified using the equation for solubility equilibrium. For a solid that dissolves in a redox reaction, solubility is expe
Blood plasma is a yellowish liquid component of blood that holds the blood cells in whole blood in suspension. In other words, it is the liquid part of the blood that carries cells and proteins throughout the body, it makes up about 55% of the body's total blood volume. It is the intravascular fluid part of extracellular fluid, it is water, contains dissolved proteins, clotting factors, hormones, carbon dioxide and oxygen. It plays a vital role in an intravascular osmotic effect that keeps electrolyte concentration balanced and protects the body from infection and other blood disorders. Blood plasma is separated from the blood by spinning a tube of fresh blood containing an anticoagulant in a centrifuge until the blood cells fall to the bottom of the tube; the blood plasma is poured or drawn off. Blood plasma has a density of 1025 kg/m3, or 1.025 g/ml. Blood serum is blood plasma without clotting factors. Plasmapheresis is a medical therapy that involves blood plasma extraction and reintegration.
Fresh frozen plasma is on the WHO Model List of Essential Medicines, the most important medications needed in a basic health system. It is of critical importance in the treatment of many types of trauma which result in blood loss, is therefore kept stocked universally in all medical facilities capable of treating trauma or that pose a risk of patient blood loss such as surgical suite facilities. Blood plasma volume may be expanded by or drained to extravascular fluid when there are changes in Starling forces across capillary walls. For example, when blood pressure drops in circulatory shock, Starling forces drive fluid into the interstitium, causing third spacing. Standing still for a prolonged period will cause an increase in transcapillary hydrostatic pressure; as a result 12% of blood plasma volume will cross into the extravascular compartment. This causes an increase in hematocrit, serum total protein, blood viscosity and, as a result of increased concentration of coagulation factors, it causes orthostatic hypercoagulability.
Plasma was well-known when described by William Harvey in de Mortu Cordis in 1628, but knowledge of it extends as far back as Vesalius.. The discovery of fibrinogen by William Henson in ca 1770 made it easier to study plasma, as ordinarily, upon coming in contact with a foreign surface – something other than vascular endothelium – clotting factors become activated and clotting proceeds trapping RBCs etc in the plasma and preventing separation of plasma from the blood. Adding citrate and other anticoagulants is a recent advance. Note that, upon formation of a clot, the remaining clear fluid is Serum, plasma without the clotting factors; the use of blood plasma as a substitute for whole blood and for transfusion purposes was proposed in March 1918, in the correspondence columns of the British Medical Journal, by Gordon R. Ward. "Dried plasmas" in powder or strips of material format were developed and first used in World War II. Prior to the United States' involvement in the war, liquid plasma and whole blood were used.
The "Blood for Britain" program during the early 1940s was quite successful based on Charles Drew's contribution. A large project began in August 1940 to collect blood in New York City hospitals for the export of plasma to Britain. Drew was appointed medical supervisor of the "Plasma for Britain" project, his notable contribution at this time was to transform the test tube methods of many blood researchers into the first successful mass production techniques. The decision was made to develop a dried plasma package for the armed forces as it would reduce breakage and make the transportation and storage much simpler; the resulting dried. One bottle contained enough distilled water to reconstitute the dried plasma contained within the other bottle. In about three minutes, the plasma could stay fresh for around four hours; the Blood for Britain program operated for five months, with total collections of 15,000 people donating blood, with over 5,500 vials of blood plasma. Following the "Plasma for Britain" invention, Drew was named director of the Red Cross blood bank and assistant director of the National Research Council, in charge of blood collection for the United States Army and Navy.
Drew argued against the armed forces directive that blood/plasma was to be separated by the race of the donor. Drew insisted that there was no racial difference in human blood and that the policy would lead to needless deaths as soldiers and sailors were required to wait for "same race" blood. By the end of the war the American Red Cross had provided enough blood for over six million plasma packages. Most of the surplus plasma was returned to the United States for civilian use. Serum albumin replaced dried plasma for combat use during the Korean War. Plasma as a blood product prepared from blood donations is used in blood transfusions as fresh frozen plasma or plasma Frozen Within 24 Hours After Phlebotomy; when donating whole blood or packed red blood cell transfusions, O- is the most desirable and is considered a "universal donor," since it has neither A nor B antigens and can be safely transfused to most recipients. Type AB+ is the "universal recipient" type for PRBC donations. However, for plasma the situation is somewhat reverse
Protein Data Bank
The Protein Data Bank is a database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data obtained by X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy, submitted by biologists and biochemists from around the world, are accessible on the Internet via the websites of its member organisations; the PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB. The PDB is a key in areas such as structural genomics. Most major scientific journals, some funding agencies, now require scientists to submit their structure data to the PDB. Many other databases use protein structures deposited in the PDB. For example, SCOP and CATH classify protein structures, while PDBsum provides a graphic overview of PDB entries using information from other sources, such as Gene ontology. Two forces converged to initiate the PDB: 1) a small but growing collection of sets of protein structure data determined by X-ray diffraction.
In 1969, with the sponsorship of Walter Hamilton at the Brookhaven National Laboratory, Edgar Meyer began to write software to store atomic coordinate files in a common format to make them available for geometric and graphical evaluation. By 1971, one of Meyer's programs, SEARCH, enabled researchers to remotely access information from the database to study protein structures offline. SEARCH was instrumental in enabling networking, thus marking the functional beginning of the PDB; the Protein Data Bank was announced in October 1971 in Nature New Biology as a joint venture between Cambridge Crystallographic Data Centre, UK and Brookhaven National Laboratory, USA. Upon Hamilton's death in 1973, Tom Koeztle took over direction of the PDB for the subsequent 20 years. In January 1994, Joel Sussman of Israel's Weizmann Institute of Science was appointed head of the PDB. In October 1998, the PDB was transferred to the Research Collaboratory for Structural Bioinformatics; the new director was Helen M. Berman of Rutgers University.
In 2003, with the formation of the wwPDB, the PDB became an international organization. The founding members are PDBe, RCSB, PDBj; the BMRB joined in 2006. Each of the four members of wwPDB can act as deposition, data processing and distribution centers for PDB data; the data processing refers to the fact that annotate each submitted entry. The data are automatically checked for plausibility; the PDB database is updated weekly. The PDB holdings list is updated weekly; as of 17 October 2018, the breakdown of current holdings is as follows: 120,052 structures in the PDB have a structure factor file. 9,734 structures have an NMR restraint file. 3,486 structures in the PDB have a chemical shifts file. 2,531 structures in the PDB have a 3DEM map file deposited in EM Data BankThese data show that most structures are determined by X-ray diffraction, but about 10% of structures are now determined by protein NMR. When using X-ray diffraction, approximations of the coordinates of the atoms of the protein are obtained, whereas estimations of the distances between pairs of atoms of the protein are found through NMR experiments.
Therefore, the final conformation of the protein is obtained, in the latter case, by solving a distance geometry problem. A few proteins are determined by cryo-electron microscopy; the significance of the structure factor files, mentioned above, is that, for PDB structures determined by X-ray diffraction that have a structure file, the electron density map may be viewed. The data of such structures is stored on the "electron density server". In the past, the number of structures in the PDB has grown at an exponential rate, passing the 100 registered structures milestone in 1982, the 1,000 in 1993, the 10,000 in 1999, the 100,000 in 2014. However, since 2007, the rate of accumulation of new protein structures appears to have plateaued; the file format used by the PDB was called the PDB file format. This original format was restricted by the width of computer punch cards to 80 characters per line. Around 1996, the "macromolecular Crystallographic Information file" format, mmCIF, an extension of the CIF format started to be phased in.
MmCIF is now the master format for the PDB archive. An XML version of this format, called PDBML, was described in 2005; the structure files can be downloaded in any of these three formats. In fact, individual files are downloaded into graphics packages using web addresses: For PDB format files, use, e.g. http://www.pdb.org/pdb/files/4hhb.pdb.gz or http://pdbe.org/download/4hhb For PDBML files, use, e.g. http://www.pdb.org/pdb/files/4hhb.xml.gz or http://pdbe.org/pdbml/4hhbThe "4hhb" is the PDB identifier. Each structure published in PDB receives a four-character alphanumeric identifier, its PDB ID; the structure files may be viewed using one of several free and open source computer programs, including Jmol, Pymol, VMD, Rasmol. Other non-free, shareware programs
A protein family is a group of evolutionarily-related proteins. In many cases a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship; the term protein family should not be confused with family. Proteins in a family descend from a common ancestor and have similar three-dimensional structures and significant sequence similarity; the most important of these is sequence similarity since it is the strictest indicator of homology and therefore the clearest indicator of common ancestry. There is a well developed framework for evaluating the significance of similarity between a group of sequences using sequence alignment methods. Proteins that do not share a common ancestor are unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein families. Families are sometimes grouped together into larger clades called superfamilies based on structural and mechanistic similarity if there is no identifiable sequence homology.
Over 60,000 protein families have been defined, although ambiguity in the definition of protein family leads different researchers to wildly varying numbers. As with many biological terms, the use of protein family is somewhat context dependent. To distinguish between these situations, the term protein superfamily is used for distantly related proteins whose relatedness is not detectable by sequence similarity, but only from shared structural features. Other terms such as protein class, group and sub-family have been coined over the years, but all suffer similar ambiguities of usage. A common usage is. Hence a superfamily, such as the PA clan of proteases, has far lower sequence conservation than one of the families it contains, the C04 family, it is unlikely that an exact definition will be agreed and to it is up to the reader to discern how these terms are being used in a particular context.. The concept of protein family was conceived at a time when few protein structures or sequences were known.
Since that time, it was found that many proteins comprise multiple independent structural and functional units or domains. Due to evolutionary shuffling, different domains in a protein have evolved independently; this has led, to a focus on families of protein domains. A number of online resources are devoted to cataloging such domains. Regions of each protein have differing functional constraints. For example, the active site of an enzyme requires certain amino acid residues to be oriented in three dimensions. On the other hand, a protein–protein binding interface may consist of a large surface with constraints on the hydrophobicity or polarity of the amino acid residues. Functionally constrained regions of proteins evolve more than unconstrained regions such as surface loops, giving rise to discernible blocks of conserved sequence when the sequences of a protein family are compared; these blocks are most referred to as motifs, although many other terms are used. Again, a large number of online resources are devoted to cataloging protein motifs.
According to current consensus, protein families arise in two ways. Firstly, the separation of a parent species into two genetically isolated descendent species allows a gene/protein to independently accumulate variations in these two lineages; this results in a family of orthologous proteins with conserved sequence motifs. Secondly, a gene duplication may create a second copy of a gene; because the original gene is still able to perform its function, the duplicated gene is free to diverge and may acquire new functions. Certain gene/protein families in eukaryotes, undergo extreme expansions and contractions in the course of evolution, sometimes in concert with whole genome duplications; this expansion and contraction of protein families is one of the salient features of genome evolution, but its importance and ramifications are unclear. As the total number of sequenced proteins increases and interest expands in proteome analysis, there is an ongoing effort to organize proteins into families and to describe their component domains and motifs.
Reliable identification of protein families is critical to phylogenetic analysis, functional annotation, the exploration of diversity of protein function in a given phylogenetic branch. The Enzyme Function Initiative is using protein families and superfamilies as the basis for development of a sequence/structure-based strategy for large scale functional assignment of enzymes of unknown function; the algorithmic means for establishing protein families on a large scale are based on a notion of similarity. Most of the time the only similarity we have access to is sequence similarity. There are many biological databases that record examples of protein families and allow users to identify if newly identified proteins belong to a known family. Here are a few examples: Pfam - Prot
Serum albumin referred to as blood albumin, is an albumin found in vertebrate blood. Human serum albumin is encoded by the ALB gene. Other mammalian forms, such as bovine serum albumin, are chemically similar. Serum albumin is produced by the liver, occurs dissolved in blood plasma and is the most abundant blood protein in mammals. Albumin is essential for maintaining the oncotic pressure needed for proper distribution of body fluids between blood vessels and body tissues, it acts as a plasma carrier by non-specifically binding several hydrophobic steroid hormones and as a transport protein for hemin and fatty acids. Too much or too little circulating serum albumin may be harmful. Albumin in the urine denotes the presence of kidney disease. Albumin appears in the urine of normal persons following long standing. Albumin functions as a carrier protein for steroids, fatty acids, thyroid hormones in the blood and plays a major role in stabilizing extracellular fluid volume by contributing to oncotic pressure of plasma.
Because smaller animals function at a lower blood pressure, they need less oncotic pressure to balance this, thus need less albumin to maintain proper fluid distribution. Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide, removed before the nascent protein is released from the rough endoplasmic reticulum; the product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a globular, water-soluble, un-glycosylated serum protein of approximate molecular weight of 65,000 Daltons. Albumin is negatively charged; the glomerular basement membrane is negatively charged in the body. According to this theory, that charge plays a major role in the selective exclusion of albumin from the glomerular filtrate. A defect in this property results in nephrotic syndrome leading to albumin loss in the urine. Nephrotic syndrome patients are sometimes given albumin to replace the lost albumin; the general structure of albumin is characterized by several long α helices allowing it to maintain a static shape, essential for regulating blood pressure.
Serum albumin contains eleven distinct binding domains for hydrophobic compounds. One hemin and six long-chain fatty acids can bind to serum albumin at the same time. Serum albumin is distributed in mammals; the human version is human serum albumin. Bovine serum albumin, or BSA, is used in immunodiagnostic procedures, clinical chemistry reagents, cell culture media, protein chemistry research, molecular biology laboratories. Human serum albumin Bovine serum albumin Blood plasma fractionation Chromatography in blood processing Lactalbumin Ovalbumin RCSB Protein Data Bank: Molecule of the Month – Serum Albumin Albumin binding prediction
In chemistry in biochemistry, a fatty acid is a carboxylic acid with a long aliphatic chain, either saturated or unsaturated. Most occurring fatty acids have an unbranched chain of an number of carbon atoms, from 4 to 28. Fatty acids are not found in organisms, but instead as three main classes of esters: triglycerides and cholesterol esters. In any of these forms, fatty acids are both important dietary sources of fuel for animals and they are important structural components for cells; the concept of fatty acid was introduced by Michel Eugène Chevreul, though he used some variant terms: graisse acide and acide huileux. Fatty acids differ by length categorized as short to long. Short-chain fatty acids are fatty acids with aliphatic tails of five or fewer carbons. Medium-chain fatty acids are fatty acids with aliphatic tails of 6 to 12 carbons, which can form medium-chain triglycerides. Long-chain fatty acids are fatty acids with aliphatic tails of 13 to 21 carbons. Long chain fatty acids are fatty acids with aliphatic tails of 22 or more carbons.
Saturated fatty acids have no C=C double bonds. They have the same formula CH3nCOOH, with variations in "n". An important saturated fatty acid is stearic acid, which when neutralized with lye is the most common form of soap. Unsaturated fatty acids have one or more C=C double bonds; the C=C double bonds can give either cis or trans isomers. Cis A cis configuration means that the two hydrogen atoms adjacent to the double bond stick out on the same side of the chain; the rigidity of the double bond freezes its conformation and, in the case of the cis isomer, causes the chain to bend and restricts the conformational freedom of the fatty acid. The more double bonds the chain has in the cis configuration, the less flexibility it has; when a chain has many cis bonds, it becomes quite curved in its most accessible conformations. For example, oleic acid, with one double bond, has a "kink" in it, whereas linoleic acid, with two double bonds, has a more pronounced bend. Α-Linolenic acid, with three double bonds, favors a hooked shape.
The effect of this is that, in restricted environments, such as when fatty acids are part of a phospholipid in a lipid bilayer, or triglycerides in lipid droplets, cis bonds limit the ability of fatty acids to be packed, therefore can affect the melting temperature of the membrane or of the fat. Trans A trans configuration, by contrast, means that the adjacent two hydrogen atoms lie on opposite sides of the chain; as a result, they do not cause the chain to bend much, their shape is similar to straight saturated fatty acids. In most occurring unsaturated fatty acids, each double bond has three n carbon atoms after it, for some n, all are cis bonds. Most fatty acids in the trans configuration are not found in nature and are the result of human processing; the differences in geometry between the various types of unsaturated fatty acids, as well as between saturated and unsaturated fatty acids, play an important role in biological processes, in the construction of biological structures. The position of the carbon atoms in a fatty acid can be indicated from the −COOH end, or from the −CH3 end.
If indicated from the −COOH end the C-1, C-2, C-3, …. Notation is used. If the position is counted from the other, −CH3, end the position is indicated by the ω-n notation; the positions of the double bonds in a fatty acid chain can, therefore, be indicated in two ways, using the C-n or the ω-n notation. Thus, in an 18 carbon fatty acid, a double bond between C-12 and C-13 is reported either as Δ12 if counted from the −COOH end, or as ω-6 if counting from the −CH3 end; the "Δ" is the Greek letter delta. Omega is the last letter in the Greek alphabet, is therefore used to indicate the “last” carbon atom in the fatty acid chain. Since the ω-n notation is used exclusively to indicate the positions of the double bonds close to the −CH3 end in essential fatty acids, there is no necessity for an equivalent “Δ”-like notation - the use of the “ω-n” notation always refers to the position of a double bond. Fatty acids with an odd number of carbon atoms are called odd-chain fatty acids, whereas the rest are even-chain fatty acids.
The difference is relevant to gluconeogenesis. The following table describes the most common systems of naming fatty acids; when circulating in the plasma are not in their ester, fatty acids are known as non-esterified fatty acids or free fatty acids. FFAs are always bound to a transport protein, such as albumin. Fatty acids are produced industrially by the hydrolysis of triglycerides, with the removal of glycerol. Phospholipids represent another source; some fatty acids are produced synthetically by hydrocarboxylation of alkenes. Template:Says whom? In animals, fatty acids are formed from carbohydrates predominantly in the liver, adipose tissue, the mammary glands during lactation. Carbohydrates are converted into pyruvate by glycolysis as the first important step in the conversion of carbohydrates into fatty acids. Pyruvate is decarboxylated to form acetyl-CoA in the mitochondrion. However, this acetyl CoA needs to be transported into cytosol where the synthesis of fatty acids occurs; this cannot occur directly.
To obtain cytosol
Apolipoproteins are proteins that bind lipids to form lipoproteins. They transport lipids in cerebrospinal fluid and lymph; the lipid components of lipoproteins are insoluble in water. However, because of their detergent-like properties and other amphipathic molecules can surround the lipids, creating a lipoprotein particle, itself water-soluble, can thus be carried through water-based circulation. In addition to stabilizing lipoprotein structure and solubilizing the lipid component, apolipoproteins interact with lipoprotein receptors and lipid transport proteins, thereby participating in lipoprotein uptake and clearance, they serve as enzyme cofactors for specific enzymes involved in the metabolism of lipoproteins. Apolipoproteins are exploited by hepatitis C virus to enable virus entry and transmission and play a role in viral pathogenesis and viral evasion from neutralizing antibodies. In lipid transport, apolipoproteins function as structural components of lipoprotein particles, ligands for cell-surface receptors and lipid transport proteins, cofactors for enzymes.
Different lipoproteins contain different classes of apolipoproteins and this influences their function. Apoplipoprotein B plays a important role in lipoprotein transport being the primary organizing protein of many lipoproteins. Apolipoprotein A-I is the major structural protein component of high-density lipoproteins, although it is present in other lipoproteins in smaller amounts. Apolipoprotein A-IV is present in chylomicrons, very-low-density lipoproteins and HDL thought to act in reverse cholesterol transport and intestinal lipid absorption via chylomicron assembly and secretion. Apolipoprotein E plays an important role in the transport and uptake of cholesterol by way of its high affinity interaction with lipoprotein receptors, including the low-density lipoprotein receptor. Apo E is the major lipoprotein in the central nervous system and has been implicated in dementia and Alzheimer's disease. Recent findings with apoA1 and apoE suggest that the tertiary structures of these two members of the human exchangeable apolipoprotein gene family are related.
The three-dimensional structure of the LDL receptor-binding domain of apoE indicates that the protein forms an unusually elongated four-helix bundle that may be stabilised by a packed hydrophobic core that includes leucine zipper-type interactions and by numerous salt bridges on the charged surface. Basic amino acids important for LDL receptor binding are clustered into a surface patch on one long helix, they are enzyme coenzymes Lipid transport proteins Ligands for interaction with lipoprotein receptors in tissues There are multiple classes of apolipoproteins and several sub-classes: apolipoprotein A apolipoprotein B apolipoprotein C apolipoprotein D apolipoprotein E apolipoprotein H apolipoprotein L apolipoproteinExchangeable apolipoproteins have the same genomic structure and are members of a multi-gene family that evolved from a common ancestral gene. ApoA1 and ApoA4 are part of the APOA1/C3/A4/A5 gene cluster on chromosome 11. Hundreds of genetic polymorphisms of the apolipoproteins have been described, many of them alter their structure and function.
Apolipoprotein synthesis in the intestine is regulated principally by the fat content of the diet. Apolipoprotein synthesis in the liver is controlled by a host of factors, including dietary composition, alcohol intake, various drugs. Apo B is an integral apoprotein. Apolipoprotein L HuGENet Review Apolipoprotein AI Mutations and Information https://patient.info/doctor/apolipoproteins