PubMed · 7869694
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A V Williams. 1994. Kidney function in congestive heart failure.. https://pubmed.ncbi.nlm.nih.gov/7869694/
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Pseudomonas aeruginosa were used for extra-cellular biosynthesis of gold nanoparticles (Au NPs). Consequently, Au NPs were formed due to reduction of gold ion by bacterial cell supernatant of P. aeruginosa ATCC 90271, P. aeruginosa (2) and P. aeruginosa (1). The UV-vis and fluorescence spectra of the bacterial as well as chemical prepared Au NPs were recorded. Transmission electron microscopy (TEM) micrograph showed the formation of well-dispersed gold nanoparticles in the range of 15-30 nm. The process of reduction being extra-cellular and may lead to the development of an easy bioprocess for synthesis of Au NPs.
Specific monitoring of recombinant protein titer in DNA recombinant biotechnology traditionally has relied on SDS-PAGE, Western blotting, or bioactivity-based assays, but these are labor-intensive, time-consuming, and destructive and are not a good choice for the optimization of recombinant protein production. We describe a study in which enhanced green fluorescence protein (EGFP) was fused to the C terminus of a model protein glutathione S-transferase (GST) to optimize the chimeric protein production in Pichia pastoris by measurements of fluorescence of living cells in a 96-well microtiter plate using simple fluorescent scanning. Several common factors (e.g., time course of expression, effect of methanol concentration, frequency of methanol addition, medium pH) were tested using this strategy. Western blotting assay showed that the correct full-length GST-EGFP chimeric protein was expressed intracellularly in P. pastoris. The fluorescence intensity and GST bioactivity of cell extract yielded a direct correlation. The results show that the reported method provides an attractive platform for the optimization of recombinant protein production in vivo in real time as well as handling at least 96 samples in parallel.
The psychrotolerant strain Pseudoalteromonas antarctica NF3, a Gram-negative bacterium isolated from muddy soil samples of Antarctica, secretes large amounts of a mucoid exopolymer with a high protein content. It has self-assembly properties and capacity to coat and protect liposomes against surfactants. We examined the ultrastructure of P. antarctica and the extracellular matter it secretes by transmission electron microscopy (TEM) after high-pressure freezing, freeze substitution (HPF-FS), and Epon embedding, and compared this with information obtained by conventional methods. The improvements brought about by HPF-FS to the ultrastructural preservation of the extracellular matter allowed us to establish for the first time, in P. antarctica NF3, the presence of two components: a large amount of cell-derived outer membrane vesicles containing proteins and a capsular polymer around the cells.