Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0267964 (PAA)
 2,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A method for specific removal of large amounts of factor IX:C alloantibodies by a resin to which highly purified factor IX was linked (factor IX CH-Sepharose) is described. Factor IX was isolated from human plasma by a three-step procedure, including barium citrate adsorption and elution, DEAE-Sepharose CL-6B chromatography, and dextran sulfate agarose chromatography. Approximately 100 mg factor IX was obtained from 60 liters of plasma. The preparation was about 95% pure as judged by SDS-PAA gel electrophoresis. Its specific coagulant activity was 160 U/mg (IX) and its factor IX clotting antigen (IX:Ag) 500-600 U/mg. Essentially quantitative coupling of the factor IX preparation to activated CH-Sepharose 4B was obtained (4 mg factor IX/ml gel; 2300-3000 U/IX:Ag/ml). This resin bound 1500-2000 U factor IX inhibitor/ml gel and could be re-used at least 5 times without any loss in binding capacity. The binding capacity was dependent on the flow rate. No signs of activation of the coagulation, fibrinolytic, or complement system were observed in vitro. Using this factor IX resin, factor IX alloantibodies were isolated and found to consist of two portions, one minor bound to the resin only in the presence of Ca2+ and another major portion Ca2+ independent. The specific inhibitory activity/milligram IgG of the Ca2+-dependent alloantibodies was about 5 times higher in the presence of Ca2+. It is concluded that 25 ml of the factor IX resin described can remove about 40,000 factor IX inhibitor units (comparable to 120,000 Bethesda U) in one run, provided the flow rate does not exceed 20 ml/hr. By using such a technique for removal of antibodies it seems feasible to convert hemophilia-B patients complicated with inhibitors against factor IX into ordinary hemophilia-B patients for treatment at an emergency or in association with major surgery.
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PMID:A technique for specific removal of factor IX alloantibodies from human plasma: partial characterization of the alloantibodies. 633 79

The preparation of stroma-free hemoglobin by selective DEAE-cellulose absorption is reported. The stroma-free hemoglobin prepared by this method is compared to the product obtained by crystallization from sodium phosphate. Both show normal serum potassium, sodium, and pH values, and no coagulant activity or blood type activity by blood type test. PAA gradient gel electrophoresis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and isoelectric focusing in polyacrylamide gel all show the same well-defined bands in both preparations. The DEAE procedure requires 11 h as compared to 4 days for the crystallization method. The recovery of hemoglobin is 77% (less than 1% methemoglobin) in the DEAE preparation compared to 34% (greater than 3% methemoglobin) by the crystallization method. In addition, far fewer expensive materials are required.
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PMID:The preparation of stroma-free hemoglobin by selective DEAE-cellulose absorption. 673 30

Using analytical PAAG-electrophoresis two specific proteins, D1 and D2, were found in decidual tissue of pregnant women (6-12 weeks). These proteins were isolated and purified by means of ammonium sulfate saturation, chromatography on Sepharose 6B and ion exchange chromatography on DEAE 52 cellulose. The degree of purification of both D1 and D2 proteins was 100% and 81%, respectively. The both proteins were free of DNA, RNA and polysaccharides. The pI values of D1 and D2 proteins were at pH 5.6-6.0. According to gel electrophoresis on PAA-SDS-Na and gel filtration on Sepharose 6B, molecular weight of D1 protein was about 50,000-55,000 and of D2 protein--150,000-160,000 and 300,000-320,000, respectively. The specific decidual proteins D1 and D2 appear to be distinct from the so-called "pregnancy proteins" described previously.
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PMID:[Isolation and purification of specific proteins, forming during endometrium differentiation into decidual tissue]. 674 Sep 97

A cellulose-based anion exchanger bearing water-soluble polycation was tested for separation of proteins. The exchanger was obtained by partial oxidation of cellulose gel by aq. NaIO4 followed by Schiff base formation with polyallylamine (PAA, molecular mass 5000). The retention behavior of proteins for three grades of PAA-cellulose gels, with amino group contents of 0.35, 0.59 and 0.96 mmol/g cellulose, was examined at several pH values and compared with that for conventional DEAE-cellulose gel with amino group content of 1.07 mmol/g cellulose. The retention of proteins by PAA-cellulose gels was remarkably greater than that for the DEAE-cellulose gel. Pairs of proteins having close isoelectric points and molecular masses (human and bovine serum albumins; beta-lactoglobulin A and B) could be separated by the PAA-cellulose gel columns. Such efficiency can be ascribed to high local density of grafted polyallylamine, in contrast to the random and sparse charge distribution in DEAE-cellulose.
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PMID:Ion-exchange separation of proteins by polyallylamine-grafted cellulose gel. 1207 22

Adsorption chromatography in expanded beds is a widely used technology for direct capture of target proteins from fermentation broths. However, in many cases this method cannot be applied as a result of the strong tendency of cells or cell debris to interact with the adsorbent beads. To prevent contamination of the expanded bed with the biomass, STREAMLINE DEAE, anion exchanger designed for expanded bed adsorption, was modified with a layer of poly(acrylic acid) (PAA). The shielding layer of polyelectrolyte was attached to the surface of the matrix beads via electrostatic interactions. PAA with a high degree of polymerization was chosen to prevent diffusion of large polymer molecules into the pores of adsorbent. Thus, the shielding layer of PAA was adsorbed only at the mouth of the pores of STREAMLINE DEAE beads and only marginally decreased the binding capacity of the ion exchanger for bovine serum albumin, the model protein in this study. PAA-coated STREAMLINE DEAE practically did not interact with yeast cells, which otherwise bound strongly to the native adsorbent at neutral conditions. Cell-resistant PAA-coated anion exchanger was successfully used for isolation of BSA from the model protein mixture containing BSA, lysozyme (positively charged at applied conditions), and yeast cells. The layer of PAA was stable under mild elution conditions, and the modified adsorbent could be used in the repeated purification cycles.
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PMID:Polyelectrolyte-coated ion exchangers for cell-resistant expanded bed adsorption. 1215 16

Identification of microbial contaminants in drinking water is a challenge to matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) due to low levels of microorganisms in fresh water. To avoid the time-consuming culture step of obtaining enough microbial cells for subsequent MALDI-MS analysis, a combination of membrane filtration and nanoparticles- or microparticles-based magnetic separation is a fast and efficient approach. In this work, the interaction of bacteria and fluidMAG-PAA, a cation-exchange superparamagnetic nanomaterial, was investigated by MALDI-MS analysis and transmission electron microscopy. FluidMAG-PAA selectively captured cells of Salmonella, Bacillus, Enterococcus and Staphylococcus aureus. This capture was attributed to the aggregation of negatively charged nanoparticles on bacterial cell regional surfaces that bear positive charges. Three types of non-porous silica-encapsulated anion-exchange magnetic microparticles (SiMAG-Q, SiMAG-PEI, SiMAG-DEAE) were capable of concentrating a variety of bacteria, and were compared with silica-free, smaller fluidMAG particles. Salmonella, Escherichia coli, Enterococcus and other bacteria spiked in aqueous solutions, tap water and reservoir water were separated and concentrated by membrane filtration and magnetic separation based on these ion-exchange magnetic materials, and then characterized by whole cell MALDI-MS. By comparing with the mass spectra of the isolates and pure cells, bacteria in fresh water can be rapidly detected at 1 x 10(3) colony-forming units (cfu)/mL.
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PMID:Interaction of bacteria and ion-exchange particles and its potential in separation for matrix-assisted laser desorption/ionization mass spectrometric identification of bacteria in water. 1991 36