Beetin
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Beetin
Beetin (BE27 or BE29) is a ribosome-inactivating protein found in the leaves of sugar beets, ''Beta vulgaris'' L, specifically attacking plant ribosomes. Sugar beet, beetins, that have been isolated meet all the criteria to be classified as single chain (type 1) ribosome inactivating proteins that are highly toxic to mammalian ribosomes but non-toxic to intact cultured mammalian cells. Beetin expression occurs when there is a viral infection of the plant. The different levels of glycosylation of the same polypeptide chain result in the two forms of beetin (BE27 or BE29). Beetin exhibits these two primary forms with apparent Mr values of 27 000 (BE27) and 29 000 (BE29) along with  possessing glycan chains. Beetins are a type-I (single-chain) proteins with N-glycoside activity. Since it has been discovered that beetin is mostly concentrated in the intercellular fluid, its presence in the remaining parts of the leaf may be below the limit of detection rather than being nonexistent. ...
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Ribosome-inactivating Protein
A ribosome-inactivating protein (RIP) is a protein synthesis inhibitor that acts at the eukaryotic ribosome. This protein family describes a large family of such proteins that work by acting as rRNA N-glycosylase (EC 3.2.2.22). They inactivate 60S ribosomal subunits by an N-glycosidic cleavage, which releases a specific adenine base from the sugar-phosphate backbone of 28S rRNA. RIPs exist in bacteria and plants. Members of the family include shiga toxins, and type I (e.g. trichosanthin and luffin) and type II (e.g. ricin, agglutinin, and abrin) ribosome inactivating proteins (RIPs). All these toxins are structurally related. RIPs have been of considerable interest because of their potential use, conjugated with monoclonal antibodies, as immunotoxins to treat cancers. Further, trichosanthin has been shown to have potent activity against HIV-1-infected T cells and macrophages. Elucidation of the structure-function relationships of RIPs has therefore become a major research effort ...
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Sugar Beets
Sugar is the generic name for sweet-tasting, soluble carbohydrates, many of which are used in food. Simple sugars, also called monosaccharides, include glucose, fructose, and galactose. Compound sugars, also called disaccharides or double sugars, are molecules made of two bonded monosaccharides; common examples are sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (two molecules of glucose). White sugar is a refined form of sucrose. In the body, compound sugars are hydrolysed into simple sugars. Longer chains of monosaccharides (>2) are not regarded as sugars, and are called oligosaccharides or polysaccharides. Starch is a glucose polymer found in plants, the most abundant source of energy in human food. Some other chemical substances, such as glycerol and sugar alcohols, may have a sweet taste, but are not classified as sugar. Sugars are found in the tissues of most plants. Honey and fruits are abundant natural sources of simple sugars. Sucrose is ...
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IRIP
iRip (formerly named iPodRip, renamed due to iPod trademark) is a commercial iPod recovery tool for Mac OS X, Windows XP and Windows Vista. It features an iTunes style interface, iPod media transfer, and integration with iTunes. It was originally released in August 2003 and has since had over 5 million downloads. iRip supports all iPods (including iPod Touch) and all iPhones. It was developed for the Hack Show during MacHack 2003. However, the developer never demonstrated it thinking the hack "too simple" when compared to Unstoppable Progress and Interface UnBuilder, both of which wowed the audience. Name change In November 2009 The Little App Factory was forced by Apple to change the name of iPodRip to remove the trademark iPod. In a bid to gain leniency the developer sent an email to Steve Jobs and this email exchange was leaked garnering headlines due to Steve's succinct reply of "Change your apps name. Not that big of a deal." The software is now known as iRip. E-Sports ...
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Saporin
Saporin is a protein that is useful in biological research applications, especially studies of behavior. Saporins are so-called ribosome inactivating proteins (RIPs), due to its N-glycosidase activity, from the seeds of ''Saponaria officinalis'' (common name: soapwort). It was first described by Fiorenzo Stirpe and his colleagues in 1983 in an article that illustrated the unusual stability of the protein. Among the RIPs are some of the most toxic molecules known, such as ricin and abrin. Each of these toxins contain a second protein subunit, which inserts the RIP into a cell, enabling it to enzymatically inactivate the ribosomes, shutting down protein synthesis, stopping basic cell functions, resulting in cell death, and eventually causing death of the victim. Saporin has no chain capable of inserting it into the cell. Thus it and the soapwort plant are safe to handle. This has aided its use in research. If given a method of entry into the cell, saporin becomes a very potent to ...
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Trichosanthin
Trichosanthin is a ribosome-inactivating protein. It is derived from ''Trichosanthes kirilowii''. It is also an abortifacient An abortifacient ("that which will cause a miscarriage" from Latin: ''abortus'' "miscarriage" and '' faciens'' "making") is a substance that induces abortion. This is a nonspecific term which may refer to any number of substances or medications, .... References External links * Proteins Ribosome-inactivating proteins {{pharmacology-stub ...
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Proteins
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 residues ...
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