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Sugar monomer and oligomer solubility: data and predictions for application to biomass hydrolysis.
Oligomer solubility could potentially play an important role in controlling the rates and yields in the thermochemical hydrolysis of hemicellulose as a pretreatment for subsequent enzymatic conversion of cellulose. However, limited data or models are available to describe the aqueous solubility of sugar monomers and oligomers. In this work, we measured the solubilities of sugars common to many biomass feedstocks in the temperature range of 25-30 degrees C. Then we reviewed solubility models for sugars from the open literature. Finally, we applied models to test their ability to describe this and other data reported in the literature. It was found that the solubility of sugar monomers was not well described by the ideal solubility law or other more complex models. However, with an empirical adjustment to the enthalpy of fusion, the ideal solubility law was able to approximately predict the solubility of cello-oligomers. Based on these results, solubilities for low molecular weight xylo-oligomers are predicted to investigate their possible importance in pretreatment and define further experimental measurements needed to improve our understanding of sugar and oligomer solubility.
Document Type:

Reference

Product Catalog Number:

20-108
Product Catalog Name:

Assay Dilution Buffer I (ADBI)
Smad proteins differentially regulate transforming growth factor-β-mediated induction of chondroitin sulfate proteoglycans.
Traumatic injury to the CNS results in increased expression and deposition of chondroitin sulfate proteoglycans (CSPGs) that are inhibitory to axonal regeneration. Transforming growth factor-β (TGF-β) has been implicated as a major mediator of these changes, but the mechanisms through which TGF-β regulates CSPG expression are not known. Using lentiviral expressed Smad-specific ShRNA we show that TGF-β induction of CSPG expression in astrocytes is Smad-dependent. However, we find a differential dependence of the synthetic machinery on Smad2 and/or Smad3. TGF-β induction of neurocan and xylosyl transferase 1 required both Smad2 and Smad3, whereas induction of phosphacan and chondroitin synthase 1 required Smad2 but not Smad3. Smad3 knockdown selectively reduced induction of chondroitin-4-sulfotransferase 1 and the amount of 4-sulfated CSPGs secreted by astrocytes. Additionally, Smad3 knockdown in astrocytes was more efficacious in promoting neurite outgrowth of neurons cultured on the TGF-β-treated astrocytes. Our data implicate TGF-β Smad3-mediated induction of 4-sulfation as a critical determinant of the permissiveness of astrocyte secreted CSPGs for axonal growth.
Document Type:

Reference

Product Catalog Number:

MAB5210
Product Catalog Name:

Anti-Phosphacan Antibody, clone 122.2
Further studies on the potential contribution of acetaldehyde accumulation and oxidative stress in rat mammary tissue in the alcohol drinking promotion of breast cancer.
There is available evidence supporting a positive association between alcohol intake and risk of breast cancer. However, there is limited information regarding possible mechanisms for this effect. Past studies from our laboratory suggest that acetaldehyde accumulation in mammary tissue after alcohol intake may be of particular relevance and that cytosolic and microsomal in situ bioactivation of ethanol to acetaldehyde and free radicals and the resulting stimulation of oxidative stress could be a significant early event related to tumor promotion. In the present studies repetitive alcohol drinking for 28 days was found to produce significant decreases in the mammary tissue content of GSH and alpha tocopherol and in glutathione S-transferase or glutathione reductase activities. In contrast, glutathione peroxidase activity was slightly increased. Malondialdehyde determinations did not show the occurrence of lipid peroxidation while the xylenol orange procedure gave positive results. The mammary microsomal metabolism of ethanol to acetaldehyde was not induced after an acute dose of ethanol or acetone able to induce the activity of its liver counterpart. The cytosolic pathway of alcohol metabolism instead was significantly enhanced by these two treatments. No increased generation of comet images was found either in mammary tissue or in liver under the experimental conditions tested. Results suggest that, while acetaldehyde accumulation in mammary tissue could be a critical event resulting from increasing production of acetaldehyde in situ plus an additional amount of it arriving via blood, other factors such as poor handling of the accumulated acetaldehyde could be also relevant.Copyright © 2010 John Wiley & Sons, Ltd.
Document Type:

Reference

Product Catalog Number:

S7101
Product Catalog Name:

ApopTag® Plus Peroxidase In Situ Apoptosis Kit