Topic
Melibiose
About: Melibiose is a research topic. Over the lifetime, 1002 publications have been published within this topic receiving 27300 citations. The topic is also known as: Melibiose.
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TL;DR: Enzymatic activities of cell-free extracts of Macracanthorhynchus hirudinaceus indicates that maltose, turanose and trehalose are hydrolyzed but with maltose being broken down four times as fast as any other disaccharide tested.
3 citations
Patent•
17 Mar 2008
TL;DR: The medium for cell culture comprises lactulose and at least one succharide selected from a group comprising raffinose, lactose, melibiose, palatinose, trehalose, Xylose, isomaltose, maltotriose, N-acetylglucosamine, xylitol, inositol, mannitol, sorbitol, maltitol, galactose, turanose and lactitol.
Abstract: PROBLEM TO BE SOLVED: To provide a culture medium for production of desired protein or proliferation of desired virus by using an animal cell, and a method for producing protein and a method for promoting proliferation of virus using these culture media.SOLUTION: There is disclosed a cell culture medium at least comprising lactulose. The medium for cell culture comprises lactulose and at least one succharide selected from a group comprising raffinose, lactose, melibiose, palatinose, trehalose, xylose, isomaltose, maltotriose, N-acetylglucosamine, xylitol, inositol, mannitol, sorbitol, maltitol, galactose, turanose and lactitol in addition to the lactulose.
3 citations
TL;DR: In this paper , the proteins modified by Melibiose-derived AGE (MAGE) were identified in human body fluids, such as serum, plasma, and peritoneal fluids.
Abstract: Melibiose-derived AGE (MAGE) is an advanced glycation end-product formed in vitro in anhydrous conditions on proteins and protein-free amino acids during glycation with melibiose. Our previous studies revealed the presence of MAGE antigen in the human body and tissues of several other species, including muscles, fat, extracellular matrix, and blood. MAGE is also antigenic and induces generation of anti-MAGE antibody. The aim of this paper was to identify the proteins modified by MAGE present in human body fluids, such as serum, plasma, and peritoneal fluids. The protein-bound MAGE formed in vivo has been isolated from human blood using affinity chromatography on the resin with an immobilized anti-MAGE monoclonal antibody. Using mass spectrometry and immunochemistry it has been established that MAGE epitope is present on several human blood proteins including serum albumin, IgG, and IgA. In serum of diabetic patients, mainly the albumin and IgG were modified by MAGE, while in healthy subjects IgG and IgA carried this modification, suggesting the novel AGE can impact protein structure, contribute to auto-immunogenicity, and affect function of immunoglobulins. Some proteins in peritoneal fluid from cancer patients modified with MAGE were also observed and it indicates a potential role of MAGE in cancer.
3 citations
TL;DR: In this article, the reaction of methanolic or aqueous ammonia with octa-O-acetyl-β-melibiose gives Nacetyl 6 O-α-D-galactopyranosyl, β-D -glucofuranosylamine (I) and 1,1-bis(acetamido)-1-deoxy-6 O-γα-d-glucitol (IV).
Abstract: The reaction of methanolic or aqueous ammonia with octa-O-acetyl-β-melibiose gives N-acetyl-6-O-α-D-galactopyranosyl-β-D-glucofuranosylamine (I) and 1,1-bis(acetamido)-1-deoxy-6-O-α-D-galactopyranosyl-D-glucitol (IV). The structure of the furanoid compound was demonstrated by oxidation with periodate. The factors which determine the different yields of these products in both media are discussed and the yields are compared with those of nitrogenated products obtained by ammonolysis of acetates of 1,4-linked disaccharides.
3 citations
TL;DR: It was concluded that the physical properties of melibiose monohydrate after storage at different RH atmospheres is largely governed by the primary particle size and porosity.
3 citations