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)

Hydrogels of poly(vinyl alcohol) (PVA), poly(acrylic acid) (PAA), and their interpenetrating networks (IPNs) were prepared using glutaraldehyde and ethylene glycol dimethacrylate as crosslinking agents. The hydrogels were characterized by measuring their equilibrium polymer volume fraction, equilibrium swelling ratio, and mesh size. Drug and protein diffusion through these hydrogels were studied. Solutes studied included theophylline, vitamin B12 and myoglobin. The ratio of PVA and PAA in the IPNs was varied to study the effect of ionic polymer content on the polymer/drug interactions and on the drug diffusion rate. Attenuated total reflectance-Fourier transform infrared (ATR-FTIR) spectroscopy was used to analyze the polymer/drug binding interactions. It was concluded that drug diffusion may be impeded by associated drug binding, especially in IPN hydrogels containing high amounts of PAA.
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PMID:Drug diffusion and binding in ionizable interpenetrating networks from poly(vinyl alcohol) and poly(acrylic acid). 970 19

Metal affinity complexes were chemically grafted onto the surface of gold matrix-assisted laser desorption/ionization (MALDI) plates by coupling a derivative of nitrilotriacetate (NTA) to immobilized poly(acrylic acid) (PAA) and subsequently forming the Fe(III)-NTA complex. The immobilized complexes can adsorb phosphorylated peptides preferentially from protein digests; deposition of digests on these surface-modified plates, followed by rinsing with an acetic acid solution, addition of matrix, and subsequent analysis by MALDI MS, resulted in mass spectra dominated by peaks corresponding to phosphopeptides. In the case of analyzing a tryptic digest of beta-casein, conventional MALDI MS revealed only one monophosphopeptide, while use of the Fe(III)-NTA-PAA-modified plate resulted in strong signals due to two additional tetraphosphorylated species. The diminution or elimination of signals due to nonphosphorylated species also greatly simplified the identification of phosphopeptides during analysis of ovalbumin digests and myoglobin digests spiked with an equimolar mixture of angiotensin and phosphoangiotensin. The matrix 2',4',6'-trihydroxyacetophenone mixed with diammonium hydrogen citrate proved to be much better than alpha-cyano-4-hydroxycinnamic acid for the detection of phosphorylated peptides from digests of beta-casein and ovalbumin.
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PMID:Detection of phosphopeptides using Fe(III)-nitrilotriacetate complexes immobilized on a MALDI plate. 1650 10

Polymeric coatings with high protein-binding capacities are important for increasing the output of affinity-based protein purification and decreasing the detection limits of antibody microarrays. This report describes the use of thick poly(acrylic acid) (PAA) brushes to immobilize as much as 80 monolayers of protein. The brushes were prepared using a recently developed procedure that allows polymerization of 100-nm-thick poly(tert-butyl acrylate) films from a surface in just 5 min along with hydrolysis of these films to PAA in 15 min. Covalent binding of bovine serum albumin (BSA) to PAA brushes that were activated using standard coupling agents, however, resulted in immobilization of less than two monolayers of BSA because of competitive hydrolysis of the esters in the activated film. In contrast, derivatization of PAA with nitrilotriacetate (NTA)-Cu2+ complexes yielded films capable of binding many monolayers of protein via metal-ion affinity interactions. For example, derivatization of 55-nm-thick PAA films with NTA-Cu2+ allowed immobilization of about 15 monolayers (5.8 microg/cm2 or 58 nm) of BSA. The binding capacity was even higher for myoglobin (7.7 microg/cm2) and anti-IgG (9.6 microg/cm2). Remarkably, electrostatic adsorption of lysozyme in 55-nm-thick, underivatized PAA resulted in as much as 80 monolayers (16.2 microg/cm2 or 162 nm) of adsorbed protein. Polymer synthesis, derivatization, and swelling, as well as BSA immobilization kinetics and thermodynamics were characterized using reflectance FT-IR spectroscopy, ellipsometry, and protein assays.
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PMID:High-capacity binding of proteins by poly(acrylic acid) brushes and their derivatives. 1661 75

Pyrolysis-gas chromatography (Py-GC) is a powerful tool for the detailed compositional analysis of polymers. A major problem of Py-GC is that polar (bio)polymers yield polar pyrolyzates which are not easily accessible to further GC characterization. In the present work, a newly developed fully automated procedure for thermally assisted hydrolysis and methylation (THM) of biopolymers is described. Drying of the sample, addition of the reagent, incubation and pyrolysis are performed inside the liner of a programmable temperature vaporizer injector. The new system not only allows efficient analysis of large series of samples, but also allows automated optimization of the experimental parameters based on an experimental design approach. The performance of the automated THM-procedure was evaluated by performing THM-GC of a poly(acrylic acid)-poly(maleic anhydride) copolymer (PAA/PMAH) and several polysaccharides. The optimized THM-procedure was applied for the structural characterization and differentiation of several lignins and hydroxypropylmethyl-celluloses. It was also applied to proteins. Here myoglobin and cytochrome c were used as the model compounds. Both conventional GC-mass spectrometry (MS) and comprehensive two-dimensional gas chromatography (GCxGC)-time-of-flight (TOF) MS were used for separation and identification of the species formed. The information obtained can aid in structure elucidation of polar biopolymers as well as in providing detailed compositional information which can be used to differentiate structurally similar biopolymers.
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PMID:Fully automated system for the gas chromatographic characterization of polar biopolymers based on thermally assisted hydrolysis and methylation. 1857 50