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Legumin
Legumin is family of globular proteins obtained from beans, peas, lentils, vetches, hemp (specifically edestin) and other leguminous seeds. Edestin is a biologically active legumin protein that is digestible for human bodies. Garden peas are a common nutritional source for humans that contains legumin. Legumin is similar to the casein of mammalian milk and was called "vegetable casein" since it was considered analogous to the mammalian protein. The primary function of the legumin protein in seeds is storage. Legumin proteins are one of the main storage proteins of angiosperms and gymnosperms. Legumin is an insoluble hexameric conjugated protein with a high concentration of carbon and oxygen. Properties Structure Legumin is a conjugated protein with six subunits. The individual subunits have a hydrophilic α chain that is initially linked to the smaller hydrophobic β chain with a peptide bond. Both the α and β chains are encoded by the same gene. Each of the six subunits ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Edestin
Edestin, (also known as Edistin) is a highly-digestible, hexameric legumin protein with six subunits, and a seed storage protein, with a molecular weight of 310 kDa. This protein is primarily found in hemp seeds. Edestin is a globular protein (biologically active) as opposed to fibrous protein (structural). Though the human body can manufacture globular proteins from any protein source, it is much more efficient for the body to make globulins from locally digestible globular proteins. Edestin has the unique ability to stimulate the manufacturing process of antibodies against invasive agents and contains a low aggravatory phosphor content (kidney ailments, etc.). Globular proteins found in edestin (and in Alpha 1 globulins, Alpha 2 globulins, Beta globulins, and Gamma globulins) are long peptide chains, precursors for biological proteins essential for life. Edestin is similar to serum globulin (blood plasma), and the biologically active protein of edestin is metabolized in the h ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Edestin
Edestin, (also known as Edistin) is a highly-digestible, hexameric legumin protein with six subunits, and a seed storage protein, with a molecular weight of 310 kDa. This protein is primarily found in hemp seeds. Edestin is a globular protein (biologically active) as opposed to fibrous protein (structural). Though the human body can manufacture globular proteins from any protein source, it is much more efficient for the body to make globulins from locally digestible globular proteins. Edestin has the unique ability to stimulate the manufacturing process of antibodies against invasive agents and contains a low aggravatory phosphor content (kidney ailments, etc.). Globular proteins found in edestin (and in Alpha 1 globulins, Alpha 2 globulins, Beta globulins, and Gamma globulins) are long peptide chains, precursors for biological proteins essential for life. Edestin is similar to serum globulin (blood plasma), and the biologically active protein of edestin is metabolized in the h ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beans
A bean is the seed of several plants in the family Fabaceae, which are used as vegetables for human or animal food. They can be cooked in many different ways, including boiling, frying, and baking, and are used in many traditional dishes throughout the world. Terminology The word "bean" and its Germanic cognates (e.g. German '' Bohne'') have existed in common use in West Germanic languages since before the 12th century, referring to broad beans, chickpeas, and other pod-borne seeds. This was long before the New World genus ''Phaseolus'' was known in Europe. After Columbian-era contact between Europe and the Americas, use of the word was extended to pod-borne seeds of ''Phaseolus'', such as the common bean and the runner bean, and the related genus ''Vigna''. The term has long been applied generally to many other seeds of similar form, such as Old World soybeans, peas, other vetches, and lupins, and even to those with slighter resemblances, such as coffee beans, vanilla b ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lentils
The lentil (''Lens culinaris'' or ''Lens esculenta'') is an edible legume. It is an annual plant known for its lens-shaped seeds. It is about tall, and the seeds grow in pods, usually with two seeds in each. As a food crop, the largest producer is Canada, producing 45% of the world’s total lentils. In cuisines of the Indian subcontinent, where lentils are a staple, split lentils (often with their hulls removed) known as dal are often cooked into a thick curry/gravy that is usually eaten with rice or ''rotis''. Botanical description Name Many different names in different parts of the world are used for the crop lentil. The first use of the word ''lens'' to designate a specific genus was in the 16th century by the botanist Tournefort. The word "lens" for the lentil is of classical Roman/Latin origin: McGee points out that a prominent Roman family took the name " Lentulus", just as the family name "Cicero" was derived from the chickpea, ''Cicer arietinum'', or " Fab ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vicilin
Vicilin is a legumin-associated globulin protein. Vicilin can be described as a storage protein found in legumes such as the pea or lentil. Vicilin is a protein that protects plants from fungi and microorganism. It has been hypothesized it's an allergen in pea allergy responses. Function of Vicilin Vicilin is a globulin present in legumes that assists the storage of proteins. Vicilins are 7S globulins. Sucrose binding, antifungal capabilities, and oxidative stress are a few of the globulin's functions. Vicilin peptides produced by digestion using trypsin or chymotrypsin offer anti-hypersensitive properties. Vicilin's function was best understood because to the addition of the copper ligand. Vicilin has various significant residues, four of which are involved in copper ion coordination. Vicilin belongs to the cupin family of proteins, therefore metal ligand coordination is common, but Vicilin is the only seed storage protein in this family known to have copper. Due to various e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Karl Heinrich Ritthausen
Karl Heinrich Ritthausen (13 January 1826 – 16 October 1912) was a German biochemist who identified two amino acids and made other contributions to the science of plant proteins. Education Ritthausen was born in Armenruh, near Goldburg, Silesia, Prussia, in today's Poland. Ritthausen's first advanced education in chemistry was in Leipzig and Bonn. He began to do research in Giessen with Justus von Liebig, and was inspired to continue investigation into agricultural chemistry. He returned to Leipzig to study with Otto Linné Erdmann. He was awarded the doctorate degree in 1853. The agricultural experiment stations at Möckern and Ida-Marienhütte were the locations of his first professional appointments. In 1862 he began to publish articles on the proteins of wheat. Protein chemistry The site of the experiment station became Poppelsdorf in 1867 when Ritthausen became professor of chemistry at University of Bonn. Working with gliadin, he identified α-aminoglutaric acid o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Coagulate
Coagulation, also known as clotting, is the process by which blood changes from a liquid to a gel, forming a blood clot. It potentially results in hemostasis, the cessation of blood loss from a damaged vessel, followed by repair. The mechanism of coagulation involves activation, adhesion and aggregation of platelets, as well as deposition and maturation of fibrin. Coagulation begins almost instantly after an injury to the endothelium lining a blood vessel. Exposure of blood to the subendothelial space initiates two processes: changes in platelets, and the exposure of subendothelial tissue factor to plasma factor VII, which ultimately leads to cross-linked fibrin formation. Platelets immediately form a plug at the site of injury; this is called ''primary hemostasis. Secondary hemostasis'' occurs simultaneously: additional coagulation (clotting) factors beyond factor VII ( listed below) respond in a cascade to form fibrin strands, which strengthen the platelet plug. Disorders of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alkalies
In chemistry, an alkali (; from ar, القلوي, al-qaly, lit=ashes of the saltwort) is a basic, ionic salt of an alkali metal or an alkaline earth metal. An alkali can also be defined as a base that dissolves in water. A solution of a soluble base has a pH greater than 7.0. The adjective alkaline, and less often, alkalescent, is commonly used in English as a synonym for basic, especially for bases soluble in water. This broad use of the term is likely to have come about because alkalis were the first bases known to obey the Arrhenius definition of a base, and they are still among the most common bases. Etymology The word "alkali" is derived from Arabic ''al qalīy'' (or ''alkali''), meaning ''the calcined ashes'' (see calcination), referring to the original source of alkaline substances. A water-extract of burned plant ashes, called potash and composed mostly of potassium carbonate, was mildly basic. After heating this substance with calcium hydroxide (''slaked lim ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Acid
In computer science, ACID ( atomicity, consistency, isolation, durability) is a set of properties of database transactions intended to guarantee data validity despite errors, power failures, and other mishaps. In the context of databases, a sequence of database operations that satisfies the ACID properties (which can be perceived as a single logical operation on the data) is called a ''transaction''. For example, a transfer of funds from one bank account to another, even involving multiple changes such as debiting one account and crediting another, is a single transaction. In 1983, Andreas Reuter and Theo Härder coined the acronym ''ACID'', building on earlier work by Jim Gray who named atomicity, consistency, and durability, but not isolation, when characterizing the transaction concept. These four properties are the major guarantees of the transaction paradigm, which has influenced many aspects of development in database systems. According to Gray and Reuter, the IBM Inf ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aspartic Acid
Aspartic acid (symbol Asp or D; the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis of proteins. Like all other amino acids, it contains an amino group and a carboxylic acid. Its α-amino group is in the protonated –NH form under physiological conditions, while its α-carboxylic acid group is deprotonated −COO− under physiological conditions. Aspartic acid has an acidic side chain (CH2COOH) which reacts with other amino acids, enzymes and proteins in the body. Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged aspartate form, −COO−. It is a non-essential amino acid in humans, meaning the body can synthesize it as needed. It is encoded by the codons GAU and GAC. D-Aspartate is one of two D-amino acids commonly found in mammals. .html" ;"title="/sup>">/sup> In proteins aspartate sidechains are often hydrogen bonded to form asx turns or asx motifs, which frequently occur at th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glutamic Acid
Glutamic acid (symbol Glu or E; the ionic form is known as glutamate) is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins. It is a non-essential nutrient for humans, meaning that the human body can synthesize enough for its use. It is also the most abundant excitatory neurotransmitter in the vertebrate nervous system. It serves as the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (GABA) in GABA-ergic neurons. Its molecular formula is . Glutamic acid exists in three optically isomeric forms; the dextrorotatory -form is usually obtained by hydrolysis of gluten or from the waste waters of beet-sugar manufacture or by fermentation.Webster's Third New International Dictionary of the English Language Unabridged, Third Edition, 1971. Its molecular structure could be idealized as HOOC−CH()−()2−COOH, with two carboxyl groups −COOH and one amino group −. However, in the solid state and mildly acidic water solut ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
