Polysaccharide labeling with

BODIPY 530/550 C3 hydrazide is 4,4-difluoro-5,7-diphenyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl hydrazide, a derivative of the basic BODIPY structure, which contains two phenyl rings off the No. 5 and 7 carbon atoms and a propionic acid hydrazide group on the No. 3 carbon atom (Molecular Probes). The hydrazide functional group reacts with aldehyde- or ketone-containing molecules to form hydrazone linkages (Fig. 229). The compound may be used to label glycoproteins or other carbohydrate-containing molecules after oxidation of their polysaccharide portions with sodium periodate to yield aldehyde residues. 

The blending chart in Fig. 1 in Chapter 5 shows an exponential dependence of solution viscosity on concentration, within the range of maximum measurable concentration (100%). Rheometry permits higher c, than does viscome-try. As a prerequisite to construction of a linear polysaccharide blending chart, the linear range of t sv/ci vs ci should first be established, because it is only then that the viscosity of the blend will be equal to the sum of the viscosities of the components. Each ordinate in Fig. 1 in Chapter 5 is labeled with the maximum ct of the two polysaccharides of interest or its equivalent as 100%. 

Tartaric acid production was accompanied by a process involving recycling of C6 of ascorbic acid into sugars and polysaccharides. When leaves were labeled with l-[ 6-ascorbic acid before anthesis, about 70% of the appeared in soluble (sugar) or residual (polysaccharide) fractions (Table II), a quantity comparable to that found in tartaric acid when the source of label was l-[1- C] ascorbic acid. The bulk of the label in the solution fraction was sucrose, glucose, and fructose while... 

Banters et al. (2003) demonstrated Cryptococcus neoformans in cerebrospinal fluid (CSF) and serum. Their 30-min procedure was based on the non-specific labelling with ChemChrome V3 in combination with a second analysis using immunofluorescence. To that end, cells were labelled with a specific primary antibody against a capsular polysaccharide and a secondary antibody conjugated with FITC. 

At equilibrium, the ratio of maltose to D-glucose is 0.52. By use of substrates labeled with carbon-14, it was diown that the reducing group of the maltose molecule is liberated as free D-glucose, and the nonreducing residue is transferred to the donor substrate. In the presence of D-glucose oxidase, equilibrium is not established, and polysaccharide which is stained blue by iodine is synthesized. Amylomaltase thus superficially resembles D-enzyme, although it must be emphasized that maltose is not a substrate for D-enzyme, which transfers two or more hexose residues at a time. 

Information on the hydrolytic activity in marine sediments has been obtained from the use of model substrates labeled with fluorescent dyes such as methylumbelliferone (MUF) or fluorescein. These substrates may be small dimeric molecules, the hydrolytic cleavage of which releases the fluorescence signal, which is then indicative of the activity of specific enzymes such as glucosidase, chitobiase, lipase, ami-nopeptidase or esterase (Chrost 1991). Also large fluorescently labeled polymers such as the polysaccharides laminarin or pullulan have been used in experiments to demonstrate the mechanism and kinetics of bacterial degradation (Amosti 1996). 

When D-glucose that has been differentially labeled with carbon-14 is supplied to plants, the labeling pattern of the D-xylose obtained by hydrolysis of the polysaccharide fraction suggests that the pentose originates... 

Cheshire, M. V., C. M. Mundie, and H. Shepherd. 1973. The origin of soil polysaccharide transformation of sugars during the decomposition in soil of plant material labelled with C. J. Soil Sci. 24 54-68. 

The polysaccharide antigen of Haemophilus influenzae type B has been labelled with tritium by use of a microculture technique using 6-[ H]-D-glucose. Fibre A -ray diffraction patterns have been interpreted for the polysaccharide from Klebsiella K57, and results indicate that the molecule has a three-fold helix with an axially projected repeat unit of 1.143 nm which correlates directly with the chemical repeat unit. ... 

Measurements of excimer or exciplex fluorescence can be used to determine whether a pair of macromolecules or two regions of a macromolecule are able to come in close contact during the lifetime of the excited state. Derivatives of pyrene that can be attached to various functional groups in proteins, lipids or polysaccharides lend themselves well to such studies [57-61]. In one application, the A-terminus of the EcoRl restriction endonuclease was labeled with N-(l-pyrenyl)iodoacetamide [62]. A broad excimer emission band at 480 nm indicated that the A-termini of two molecules come into close proximity when the protein dimerizes. The A-termini are essential for enzymatic activity but are too disordered to be seen in a crystal structure of the protein. 

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