Flatbed
Mostrando 13-17 de 17 artigos, teses e dissertações.
-
13. Purification and characterization of heat-stable enterotoxin from bovine enterotoxigenic Escherichia coli.
Heat-stable enterotoxin (ST) from Escherichia coli pathogenic for cattle was mass produced in a chemically defined medium. The toxin was concentrated and purified by sequentially applying batch adsorption chromatography on Amberlite XAD-2 resin, acetone fractionation, and preparative isoelectric focusing in a flatbed granulated gel. Reverse-phase high-perfor
-
14. Comparison of platelet storage in PL146 and PL732 plastic packs: preliminary in vitro studies.
This paper is a preliminary report of in vitro studies comparing platelet storage in the new polyolefin PL732 packs with the present polyvinyl PL146 packs. The parameters used to assess platelet viability in these studies were the recovery from the hypotonic stress test (HST) and the pH. The effect of the mass of concentrate was assessed by preparing 20 g, 3
-
15. Purification and Characterization of a Serratia marcescens Metalloprotease
An extracellular, nonelastolytic, neutral metalloprotease of Serratia marcescens was purified by sequential ammonium sulfate precipitation, hydroxyapatite adsorption chromatography, flat-bed isoelectric focusing, and Sephadex G-100 gel filtration. The protease preparation had a 280/260 nm absorbance ratio of 1.8, was free of detectable amounts of endotoxin,
-
16. Purification of Pseudomonas aeruginosa proteases and microscopic characterization of pseudomonal protease-induced rabbit corneal damage.
Extracellular proteases of three cornea-virulent strains of Pseudomonas aeruginosa were isolated by sequential ammonium sulfate precipitation, Ultrogel AcA 54 gel filtration, and flat-bed isoelectric focusing. The purity of the preparations was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis , thin-layer isoelectric focusing in polyac
-
17. Adenylate cyclase activity of a 68,000-molecular-weight protein isolated from the outer membrane of Bordetella bronchiseptica.
A method was developed which is suitable for the isolation of substantial quantities of outer membrane proteins of Bordetella species in a water-soluble form. The extracted material may then be further fractionated in the absence of detergents by ion-exchange chromatography and preparative flat-bed isoelectrofocusing. These procedures facilitated the isolati