The protein patterns showed a high abundance of protein spots in the acidic range, including three lectin proteins. The metabolic and defense enzymes, such as superoxide dismutase (SOD) and ascorbate peroxidase, that are associated with antioxidant activity, were mainly found in the basic region. Furthermore, cysteine protease was found in this plant, as had been previously reported in other Zingiberaceae plants.\n\nConclusion: This report presents the protein profiles of the ginger plant, Curcuma comosa. Several interesting 123 proteins were identified in

this plant that may be used as a protein marker and aid in identifying plants of the Zingiberaceae family.”
“On many occasions, homopolysaccharide hydrogel networks alone are not suitable for controlled drug delivery. In this study, interpenetrating networks (IPNs) of sodium alginate (ALG) and etherified BI 2536 in vitro locust bean gum (ELBG) were developed through ionotropic gelation with Al3+ ions, tested for glipizide release, and were compared with homopolymer hydrogel networks. The degree of reticulation in IPNs was explained by the neutralization equivalent, tensile

strength measurement, and drying DAPT kinetics of drug-free hydrogels. IPNs afforded a maximum of 94.40 +/- 0.35% drug entrapment efficiency and exhibited slower drug release profiles up to 8h. Al3+-ALG network almost completed the release of embedded drug in 3.5h; however, the homopolymer Al3+-ELBG network discharged their content at a slow, uniform rate up to 8h like the IPNs. All the networks appeared spherical under scanning electron microscope. In all cases, JQ1 molecular weight a faster drug release rate was assumed in phosphate buffer (pH 7.4) than in KCl/HCl buffer (pH 1.2) solution. The pH-responsive swelling of the beads was responsible for the variable drug release rate in different media. NonFickian diffusion mechanism was operative for the transport of drug from the IPNs. Moreover, IPNs gained appreciation for their better mechanical strength (63.79 +/- 1.59MPa) than Al3+-ELBG network. Fourier transform infrared (FTIR) spectroscopy, differential scanning

calorimetry, and X-ray diffraction analyses indicated a compatible environment for drug encapsualtion and release from the IPNs. The drug release curves of Al3+-ELBG and IPNs were found similar to a reference product. Hence, Al3+-ELBG and IPNs could be useful in controlling diabetes over longer periods.”
“The Omp85/TPS (outer-membrane protein of 85 kDa/two-partner secretion) super-family is a ubiquitous and major class of beta-barrel proteins. This superfamily is restricted to the outer membranes of gram-negative bacteria, mitochondria, and chloroplasts. The common architecture, with an N-terminus consisting of repeats of soluble polypeptide-transport-associated (POTRA) domains and a C-terminal beta-barrel pore is highly conserved.