Authors:Michaela Bleichert, Hanns-Simon Eckhardt, Karl-Friedrich Klein, and Bernd Spangenberg
HPTLC on amino plates, with simple heating of the plates for derivatization, has been used for quantification of glucosamine in nutritional supplements. On heating the plate glucosamine reacts to form a compound which strongly absorbs light between 305 and 330 nm, with weak fluorescence. The reaction product can be detected sensitively either by absorption of light or by fluorescence detection. The detection limit in absorption mode is approximately 25 ng per spot. In fluorescence mode a detection limit of 15 ng is achievable. A calibration plot for absorption detection is linear in the range 25 to 4000 ng glucosamine. The derivative formed from glucosamine by heating is stable for months, and the relative standard deviation is 1.64% for 600 ng glucosamine. The amounts of glucosamine found in nutritional supplements were in agreement with the label declarations.
Authors:Chuan-Min Qi, Yong He, Xiao Wang, Man Feng, Jing-Li Xu, Rui Ding, Hang Liu, Yu-Rong Chen, Fang Li, Zhao-Hui Zhu, Yong-Hong Dang, Shu-Ting Zhang, and Ying Xie
d-glucosamine at concentration of certain range could kill tumor cells without influencing normal cells. There are also some
reports on the antitumor activity of d-glucosamine and its derivatives in murine models. It was therefore postulated that d-glucosamine might have the potential to invade tumor cells. We designed and radiosynthesized a glucosamine derivative, N-(2-[18F]fluoro-4-nitrobenzoyl)glucosamine ([18F]FNBG([18F]7)). Evaluations in vitro and in vivo were performed on tumor bearing mice. Excitingly, the radiochemical purity of [18F]FNBG([18F]7) was 99%, and besides the best radiochemical yield was up to 35%. The best T/Bl (Tumor/Blood) and T/M (Tumor/Muscle) ratios
of [18F]FNBG([18F]7) were 4.40 and 4.84. Although [18F]FNBG([18F]7) deserved further studies, the results revealed it might become a potential PET imaging agent for detecting tumors.
Authors:S. Mondal, M. Berihun, M. Kovacs, G. Vatai, and A. Koris
, S.M. , Minasaki , R. , Farrell , R.L. , Thwaites , J.M. , Held , B.W. … & Aiba , S. ( 2003 ): Enzymatic production of N-acetyl-D-glucosamine from chitin: Degradation study of N-acetylchitooligosaccharide and the
Authors:Mária Hevesi, Ágnes Móricz, Zsuzsa Király-Véghely, Magdolna Tóth, György Kátay, and Ernő Tyihák
On the basis of our earlier observations, preliminary experiments were conducted with the fire blight pathogen Erwinia amylovora with the BioArena system using the potential antibacterial substances 1′-methylascorbigen (MeAG) as formaldehyde (HCHO) precursor and trans-resveratrol (RES) as HCHO mobilizer, capturer, and scavenger. Results showed characteristic, strong, dose-dependent antibacterial effects of both MeAG and RES present as chromatographic spots on the adsorbent layer. It is supposed that the weak antibacterial effect of AG may have originated from MeAG formed in situ on the layer by partial enzymatic methylation of AG. Addition of HCHO capture compounds (l-arginine, glutathione, glucosamine) to the culture medium before inoculation partially or totally reduced the antibacterial effect of both molecules, that is, this simplest aliphatic aldehyde, the endogenous HCHO molecule, participates in the antibacterial activity of these compounds. It follows from these results that there is a possibility of interaction between endogenous H2O2 and HCHO in the chromatographic spots and it is supposed that these reactive molecules and potential derivatives, e.g. singlet oxygen (1O2) and ozone (O3), may be the causes of the destructive effect of the fire blight pathogen on fruit trees.
Adhesion to target cells is an essential step in the pathogenesis of many protozoal infections. Some protozoa have been reported to have a lectin activity involved in their attachment to the cell surface. The ligand-receptor interaction involved in Theileria annulata infection is unclear at present, in spite of the fact that some aspects of the process have been investigated. To this end, T. annulata piroplasms have been screened for lectin activity. Blood taken from infected cattle was first depleted of leukocytes and then subjected to ammonium chloride lysis in order to isolate the piroplasms. The piroplasms were homogenised and a crude membrane extract was prepared by centrifugation. To investigate lectin activity in piroplasm proteins, a simple screening procedure was employed for analysing piroplasm proteins binding to various lectin ligands. Numerous immobilised lectin ligands (L-fucose-sepharose, N-acetyl-neuraminic acid-sepharose, N-acetyl-D-galactosamine-agarose, N-acetyl-D-glucosamine-agarose, D-mannose-agarose, β-D-glucose-agarose, α-methyl-D-mannoside-agarose) were incubated with T. annulata piroplasm crude membrane extract. The ligand-bound proteins were eluted and separated by a brief centrifugation and determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The present study suggests that a 32 kDa protein of piroplasm binds to D-galactosyl residues of the agarose matrix and that the binding is inhibited by galactose and not by the other monosaccharides tested.