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Vicilin
Vicilin is a legumin-associated globulin protein. It is a storage protein found in legumes such as the pea or lentil that protects plants from fungi and microorganism. It is believed to be an allergen in pea and peanut 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, in which metal ligand coordination is common, but vicilin is the only seed storage protein in this family known to include copper. This inclusion is crucial for enzymatic activity. Vicili ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Legumin
Legumin is family of globular proteins obtained from beans, peas, lentils, vetches, Hemp protein, hemp and other leguminous seeds. 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 Flowering plant, 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 has a mass of ~50-60 kDa. During Translation (biology), translation of the α and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Globulin
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. Types of globulin All globulins fall into one of three categories: * Alpha 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 gl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Legume
Legumes are plants in the pea family Fabaceae (or Leguminosae), or the fruit or seeds of such plants. When used as a dry grain for human consumption, the seeds are also called pulses. Legumes are grown agriculturally, primarily for human consumption, but also as livestock forage and silage, and as soil-enhancing green manure. Legumes produce a botanically unique type of fruit – a simple fruit, simple Dry fruits, dry fruit that develops from a simple carpel and usually Dehiscence (botany) , dehisces (opens along a seam) on two sides. Most legumes have Symbiosis , symbiotic nitrogen fixation , nitrogen-fixing bacteria, Rhizobia, in structures called root nodules. Some of the fixed nitrogen becomes available to later crops, so legumes play a key role in crop rotation. Terminology The term ''pulse'', as used by the United Nations' Food and Agriculture Organization (FAO), is reserved for legume crops harvested solely for the dry seed. This excludes green beans and Pea , green ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lentil
The lentil (''Vicia lens'' or ''Lens culinaris'') is an annual plant, annual legume grown for its Lens (geometry), lens-shaped edible seeds or ''pulses'', also called ''lentils''. It is about tall, and the seeds grow in Legume, pods, usually with two seeds in each. Lentil seeds are used around the world for culinary purposes. In cuisines of the Indian subcontinent, where lentils are a staple food, staple, split lentils (often with their hulls removed) known as ''dal'' are often cooked into a thick curry that is usually eaten with rice or roti. Lentils are commonly used in stews and soups. 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 17th century by the botanist Joseph Pitton de Tournefort, Tournefort. The word "lens" for the lentil is of classical Roman or Latin origin, possibly from a prominent Roman family named Lentulus, just as ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fungus
A fungus (: fungi , , , or ; or funguses) is any member of the group of eukaryotic organisms that includes microorganisms such as yeasts and mold (fungus), molds, as well as the more familiar mushrooms. These organisms are classified as one of the kingdom (biology)#Six kingdoms (1998), traditional eukaryotic kingdoms, along with Animalia, Plantae, and either Protista or Protozoa and Chromista. A characteristic that places fungi in a different kingdom from plants, bacteria, and some protists is chitin in their cell walls. Fungi, like animals, are heterotrophs; they acquire their food by absorbing dissolved molecules, typically by secreting digestive enzymes into their environment. Fungi do not photosynthesize. Growth is their means of motility, mobility, except for spores (a few of which are flagellated), which may travel through the air or water. Fungi are the principal decomposers in ecological systems. These and other differences place fungi in a single group of related o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Microorganism
A microorganism, or microbe, is an organism of microscopic scale, microscopic size, which may exist in its unicellular organism, single-celled form or as a Colony (biology)#Microbial colonies, colony of cells. The possible existence of unseen microbial life was suspected from antiquity, with an early attestation in Jain literature authored in 6th-century BC India. The scientific study of microorganisms began with their observation under the microscope in the 1670s by Anton van Leeuwenhoek. In the 1850s, Louis Pasteur found that microorganisms caused food spoilage, debunking the theory of spontaneous generation. In the 1880s, Robert Koch discovered that microorganisms caused the diseases tuberculosis, cholera, diphtheria, and anthrax. Microorganisms are extremely diverse, representing most unicellular organisms in all three domains of life: two of the three domains, Archaea and Bacteria, only contain microorganisms. The third domain, Eukaryota, includes all multicellular o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oxidative Stress
Oxidative stress reflects an imbalance between the systemic manifestation of reactive oxygen species and a biological system's ability to readily detoxify the reactive intermediates or to repair the resulting damage. Disturbances in the normal redox state of cells can cause toxic effects through the production of peroxides and free radicals that damage all components of the cell, including proteins, lipids, and DNA. Oxidative stress from oxidative metabolism causes base damage, as well as strand breaks in DNA. Base damage is mostly indirect and caused by the reactive oxygen species generated, e.g., (superoxide radical), OH ( hydroxyl radical) and (hydrogen peroxide). Further, some reactive oxidative species act as cellular messengers in redox signaling. Thus, oxidative stress can cause disruptions in normal mechanisms of cellular signaling. In humans, oxidative stress is thought to be involved in the development of attention deficit hyperactivity disorder, cancer, Parkin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Trypsin
Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins. Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. It is used for numerous biotechnological processes. The process is commonly referred to as trypsinogen proteolysis or trypsinization, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin was discovered in 1876 by Wilhelm Kühne. Although many sources say that Kühne named trypsin from the Ancient Greek word for rubbing, 'tripsis', because the enzyme was first isolated by rubbing the pancreas with glass powd ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chymotrypsin
Chymotrypsin (, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum, where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid N-terminal to the scissile amide bond (the P1 position) is a large hydrophobic amino acid ( tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their side chain that fits into a hydrophobic pocket (the S1 position) of the enzyme. It is activated in the presence of trypsin. The hydrophobic and shape complementarity between the peptide substrate P1 side chain and the enzyme S1 binding cavity accounts for the substrate specificity of this enzyme. Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycerol
Glycerol () is a simple triol compound. It is a colorless, odorless, sweet-tasting, viscous liquid. The glycerol backbone is found in lipids known as glycerides. It is also widely used as a sweetener in the food industry and as a humectant in pharmaceutical formulations. Because of its three hydroxyl groups, glycerol is miscible with water and is Hygroscopy, hygroscopic in nature. Modern use of the word glycerine (alternatively spelled glycerin) refers to commercial preparations of less than 100% purity, typically 95% glycerol. Structure Although chirality, achiral, glycerol is prochirality, prochiral with respect to reactions of one of the two primary alcohols. Thus, in substituted derivatives, the Glycerophospholipid#Nomenclature and stereochemistry, stereospecific numbering labels the molecule with a ''sn''- prefix before the stem name of the molecule. Production Natural sources Glycerol is generally obtained from plant and animal sources where it occurs in triglycerides, est ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metab ... or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus. Chemistry Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
