This review summarizes common and distinct features among Nef proteins and how they contribute to increasing HIV and Sly fitness towards their respective hosts. (C) 2010 Elsevier Ltd. All rights reserved.”
“Oil bodies, with their unique structural proteins, oleosins, are known to be useful in foods and other emulsion systems. The influence of kappa, iota, and lambda-carrageenans on the stability of soybean oil body emulsions at different pH values (pH 3, 4, 5 and 7) was investigated by particle electrical charge, particle size distribution, creaming stability and confocal laser scanning

microscopy measurements. In acidic environment (pH 3, 4 and 5), the droplet charge of soybean oil body emulsions stabilized with carrageenan decreased with increasing carrageenan concentration for all types of carrageenan investigated, suggesting their adsorption to the oil body droplet surfaces. Extensive droplet aggregation and creaming were AC220 chemical structure observed in the emulsions stabilized see more with lambda-carrageenan at pH 3 and 5, indicating that soybean oil body droplets were bridged by carrageenan. At pH 7, there was no significant change in the droplet charge of soybean

oil body emulsions stabilized with three types of carrageenan, but the emulsions stabilized with iota-carrageenan were more stable to creaming due to depletion flocculation than the emulsions stabilized with kappa or lambda-carrageenan after seven days storage. The probable reason was that iota-carrageenan, which had the most densely AZD1208 in vivo charged helical structure, was most effective at creating highly

charged interfacial membranes, thus reducing the depletion flocculation to occur. (C) 2011 Elsevier Ltd. All rights reserved.”
“Yellow pea seed protein-derived peptides were produced through enzymatic hydrolysis of pea protein isolate, which was followed by ultrafiltration to isolate peptides with <3 kDa sizes (PPH). The PPH was separated by cation-exchange chromatography into five peptide fractions (F1-F5) based on their affinity for the stationary phase. F1 contained peptides with the least amount (7.5%) of cationic amino acids while F5 contained peptides with more than 50% content of cationic amino acids. F1-F5 peptide fractions were evaluated for in vitro antioxidant activities in comparison to glutathione (GSH), an endogenous antioxidant peptide. Results showed that the peptide fraction with the least cationic property (F1) had significantly strongest (p<0.05) scavenging activity against 1,1-diphenyl-2-picrylhydrazyl radical and hydrogen peroxide (H(2)O(2)) when compared to F2-F5. Generally, the scavenging of O(2)(center dot-) and H(2)O(2) was negatively related with the cationic property of the peptide fractions. Fractionation according to cationic property resulted in significantly increased (p<0.05) O(2)(center dot-) scavenging power of the peptide fractions (F1-F5) when compared to the unfractionated PPH.