Anagram & Information om | Engelska ordet LECTINS

Exempel på hur man kan använda LECTINS i en mening

• Carbohydrate bonding is most often used with glycoproteins or any other carbohydrate-containing substance; carbohydrate is used with lectins, glycoproteins, or any other carbohydrate metabolite protein.
• lectins, streptavidin, monoclonal antibodies, phospholipase A2 and acetylcholinesterase, tailoring of bioreactive surfaces; mixed protein multilayers.
• The beads are coated with primary antibodies, specific-specific antibodies, lectins, enzymes, or streptavidin; the linkage between magnetized beads coated materials are cleavable DNA linker cell separation from the beads when the culturing of cells is more desirable.
• All selectins are single-chain transmembrane glycoproteins that share similar properties to C-type lectins due to a related amino terminus and calcium-dependent binding.
• Components of the elderberry plant, including its fruit, contain diverse phytochemicals, such as alkaloids, lectins, and cyanogenic glycosides, which may be toxic if consumed raw.
• The asialoglycoprotein receptors (ASGPR) are lectins which bind asialoglycoprotein and glycoproteins from which a sialic acid has been removed to expose galactose residues.
• Siglecs (Sialic acid-binding immunoglobulin-type lectins) are cell surface proteins that bind sialic acid.
• In contrast to other lectins, for instance, DC-SIGN / DC-SIGNR and MBP, langerin has only one binding site for Ca2+.
• Surfactant protein D, also known as SP-D, is a lung surfactant protein part of the collagenous family of lectins called collectin.
• He is also exploring the roles of proteins and lectins that recognize glycans, as well as anti-glycan antibodies, in biological pathways and disease, including inflammation, autoimmunity, infectious diseases, and cancer.
• The lectins, calnexin and calreticulin, have high affinities for monoglucosylated proteins and the ER chaperones that associate with these lectins assist the folding of the misfolded glycoprotein.
• In this field of Glycobiology, his present focus is on the Sialic Acids, which are found at the outermost position on such glycans, and which can be recognized by intrinsic receptors such as Selectins and the Siglecs (which he co-discovered and named as a sub-group of I-type Lectins), and also by the binding proteins of various pathogens.
• Furthermore, the terminal saccharide in glycan chains can serve to function in specific ligand interactions with lectins(carbohydrate binding molecules), these lectins can originate from the host and can interact with the terminal saccharides of a glycan chain in a specific process or they can originate from pathogens and interact with terminal saccharides to aid in pathogen entry into cells.
• Pathogen-associated molecular pattern (PAMPs) and damage-associated molecular pattern (DAMPs) are often identified by lectins which is a protein that binds specific carbohydrates.
• as a technique which probes proteins blotted to polyvinylidene fluoride membrane with lectins, cholera toxin and chemical stains to detect glycosylated, lipoylated or phosphorylated proteins.
• Jacalin belongs to a family of galactose-binding lectins containing the Jacalin-like lectin domain and it has a tetrameric two-chain structure with a weight of 66 kDa.
• All jacalin-related lectins feature type I beta-prism folding motifs (the beta-prism I fold is like a perfect beta-prism with each side made up of a four-stranded greek key motif), but BanLec is the first jacalin-related lectin from the monocot family of plants, while all other members are dicots; other monocot mannose-binding lectins exhibit beta-prism II folding instead.
• These fungal lectins, such as Aleuria aurantia lectin AAL, specifically recognise fucosylated glycans.
• Some lectins in this group stimulate distinct T- and B-cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin.
• He genetically re-engineered carbohydrate specificities of lectins imparting T-antigen tumor recognizing ability to peanut agglutinin.

Förberedelsen av sidan tog: 221,72 ms.