Sugar gradient

There is no particular nutrient value in sugar, except when the bacterium is crossing the sugar gradient and its metabolism utilizes the molecule so as to permit the continuity of its identity. 

PR proteins Reactive oxygen species Sugar gradient ... 

When sugar gradient-elution is used for saccharide desorption the range and steepness of the gradient needs to be adapted to the experimental conditions. A useful linear gradient for preliminary studies would extend from 0—0.2 M sugar in equilibration buffer, in a total volume of 100 ml. One ml fractions should be collected at a flow-rate of 10 ml/h. 

The gradients of H, Na, and other cations and anions established by ATPases and other energy sources can be used for secondary active transport of various substrates. The best-understood systems use Na or gradients to transport amino acids and sugars in certain cells. Many of these systems operate as symports, with the ion and the transported amino acid or sugar moving in the same direction (that is, into the cell). In antiport processes, the ion and the other transported species move in opposite directions. (For example, the anion transporter of erythrocytes is an antiport.) Proton symport proteins are used by E. coU and other bacteria to accumulate lactose, arabinose, ribose, and a variety of amino acids. E. coli also possesses Na -symport systems for melibiose as well as for glutamate and other amino acids. 

Glucose transporters are integral membrane proteins that catalyze the permeation of sugars into cells, along or against a concentration gradient. 

Sixteen solid-phase materials were tested on a laboratory scale and the antho-cyanin and sugar content of collected fractions were determined. Among these, reverse-phase silica gels and macroreticular non-ionic acrylic polymer adsorbents such as Serdolit PAD IV or Amberlite XAD-7 turned out to be most suitable. SPE was used to investigate these materials on an enlarged scale, improving elution gradient and column purification. Amberlite XAD-7 was successfully applied in a middle-scale separation. ... 

Figure 3. Anion-exchange chromatography on DEAE Sepharose of fraction I of the Sephacryl S300 fractionation of a) saponified MHR population A after degradation with RGase and after b) degradation of the non-saponified MHR population A with RGase and RGAEase ---------, uronic acid —, neutral sugars thin line, NaOAc gradient [39],...

ChSS was fractionated on a column (550 x 15 mm) of DEAE Sepharo e Fast Flow using a Hiload System (Pharmacia), which was initially equilibrated in 0.005 M NaAc-bufFer pH 5.0. The sample was dissolved in water, the insoluble residue was removed by centrifugation and the supernatant was applied onto the column. After applying the gradient shown in Figure 1, the residual polysaccharides were washed from the column using 0.5 M NaOH. Fractions (23 ml) were collected and assayed by automated methods [2,3] for total neutral sugars and uronic acids. 

Figure 2. CM-cellulose chromatography of pectolytic enzymes. The activity peaks of the flow-through of a DEAE-cellulose chromatography was applied to a CM-cellulose column. The column was eluted with a NaCl (0-0.5M) continuous gradient at a flow rate of 34 ml/h. 10 ml fractions were collected and assayed for pectolytic activities Symbols (0) pectate lyase ( ) polygalacturonase (reducing sugar-releasing activity) (x) protein. Other details in Methods.

Osmosis The movement of water against a sugar concentration gradient through a semi-... 

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