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)

PP10 was isolated from aqueous extracts of human term placentae by fractionating the proteins with rivanol and ammonium sulfate, by gelfiltration on Sephadex G-150 and by use of immunoadsorbents. PP10 apparently is a protein specific for the placenta; it could not be detected in extracts from other human tissues. From one human term placenta an average amount of 20 mg PP10 can be extracted. In sera from pregnant women PP10 is usually present only in trace amounts (less than 0.1 mg/100 ml). PP10 has the electrophoretic mobility of an alpha1-globulin and an isoelectric point of 5.1. The purified protein sediments with 3.8 S. PP10 was found to have a molecular weight of 48,000 as determined by ultracentrifugation and a molecular weight of 65,000 as determined by SDS-PAA gel electrophoresis. PP10 is a glycoprotein containing 6.65% carbohydrates (hexoses 4.8%, hexosamines 1.2%, fucose 0.05%, sialic acid 0.6%). The amino acid composition of PP10 has been determined, too; the most abundant amino acids in this protein are glutamic acid, aspartic acid, leucine and alanine.
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PMID:[Isolation and characterization of a new placenta specific protein (PP10) (author's transl)]. 48 20

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

The ability of four different 40% poly(acrylic acid) (PAA) solutions, containing 4 or 6 wt-% of either Na2SO4 or (NH4)2SO4, to cause precipitation of CaSO4 on dentin surfaces was investigated. Each treatment consisted of exposing the dentin to one of the four solutions for either 1 or 2 min and was followed by a water rinse (1 min) and air drying (30 sec). The treated dentin surfaces were then evaluated in a scanning electron microscope (SEM), which showed that crystals precipitated on the dentin with these solutions. Of the four investigated PAAs, one performed better than the others with regard to crystal precipitation and blockage of the tubules. This solution was selected for additional studies of the effects of different PAA concentrations (10%, 20%, 30%, 40%, and 50%). In these solutions, 4 and 6 wt-% of either Na2SO4 or (NH4)2SO4 were dissolved. Additional dentin surfaces were then treated with these solutions as described earlier and evaluated in an SEM. This evaluation showed that solutions containing 30-50% PAA resulted in optimized crystal formation for all the different sulfate solutions and that the optimization occurred within 1 min. Besides optimizing crystal precipitation, these mixtures also minimized the frequency of open dentinal tubules.
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PMID:Crystal precipitation on dentin by poly(acrylic acid) solutions containing SO4(2-) ions. 830 12

The uptake characteristics of negatively-charged liposomes made by conjugation of poly(acrylic acid) (PAA) were studied with respect to cultured RAW macrophages. The PAA-conjugated liposomes were internalized and digested in an acidic compartment at a much faster rate than the unmodified phosphatidylcholine (PC) liposomes. After incubation for 18 h, an over 5-fold increase in the uptake of PC liposomes was obtained by PAA conjugation. Subsequently, part of the aqueous phase of the internalized liposomes was exocytosed. Recognition of PAA by the macrophages seems to be responsible for the enhanced uptake of PAA-conjugated liposomes. Cross-competition experiments showed that PAA-conjugated liposomes inhibited the uptake of acetylated-low density lipoprotein (acetyl-LDL) by the macrophages and vice versa. The uptake of PAA-conjugated liposomes was also inhibited by dextran sulfate and maleylated-bovine serum albumin (maleyl-BSA), which are also known to bind to scavenger receptors. Poly(C) and BSA, which are not ligands for the scavenger receptor, competed poorly with the uptake of PAA-conjugated liposomes. Enhanced uptake of PAA-conjugated liposomes by CHO cells with low scavenger receptor expression was not observed. Unexpectedly, LDL, which is not a ligand for scavenger receptor, also partially inhibited the uptake of PAA-conjugated liposomes. The interaction of PAA-conjugated liposomes with macrophages is complex, and the endocytosis of PAA-conjugated liposomes most likely involves multiple receptors and/or pathways. The data obtained suggest that the high affinity binding of PAA-conjugated liposomes to macrophages may be due to recognition of the negative charges of PAA by cell surface receptors, including the scavenger receptor.
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PMID:Receptor-mediated endocytosis of poly(acrylic acid)-conjugated liposomes by macrophages. 861 8

Of the several existing methods for quantification of major subspecies of high density lipoprotein (HDL), HDL2 and HDL3, the methods based upon double precipitation are particularly useful for large-scale studies or for routine assay because of their high speed and low cost. The Vertical Auto Profile-II (VAP-II) method developed in our laboratory primarily for the direct single test measurement of cholesterol (C) in all major lipoproteins, including Lp[a] and IDL, is rapid, highly sensitive, and suitable for large-scale studies. Here we describe the modification of this procedure so as to be able to quantify both HDL2- and HDL3-C in addition to all major lipoproteins without any additional assay steps, time, or cost. The VAP-II procedure was validated by comparison with four other methods using plasma samples obtained from 35 healthy subjects: 1) HDL-VAP-II (a variation of the VAP-II procedure designed specifically to separate HDL subspecies); 2) dextran sulfate (DS)/Mg2+ double precipitation method performed at Northwest Lipid Research Laboratories (NWLRL), Seattle, WA; 3) 4-30% polyacrylamide-agarose (4/30 PAA) nondenaturing gradient gel electrophoresis (GGE); and 4) analytical ultracentrifugation (AUC), with both GGE and AUC performed at the Donner Laboratory, University of California at Berkeley. Both HDL2- and HDL3-C measurements by VAP-II correlated well with the measurements by all comparison methods (r for HDL3-C: HDL-VAP-II, 0.948; NWLRL, 0.947; GGE, 0.861; and AUC, 0.706, and r for HDL2-C: HDL-VAP-II, 0.867; NWLRL, 0.854; GGE, 0.885; and AUC, 0.721). The measurements of HDL2- and HDL3-C by the VAP-II method are reproducible, with the long-term between-rotor CV of 5.0% for HDL3-C and 9.0% for HDL2-C.
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PMID:Quantification of HDL2 and HDL3 cholesterol by the Vertical Auto Profile-II (VAP-II) methodology. 939 33

The ability of tetrasaccharides (SiaLex, SiaLea, HSO3Lex), their conjugates with polyacrylamide (40 kDa), and several other monomeric and polymeric substances to block selectins has been compared with that of polysaccaride fucoidan. Two assay systems were used: one was constructed on the base of recombinant E-, P-, and L-selectins; the other was a rat model of peritoneal inflammation. IC50 values for the neoglycoconjugate SiaLea-PAA were 6, 40, and 85 microM with the recombinant E-, P-, and L-selectins, respectively; all monomeric inhibitors were about two orders of magnitude weaker. PAA-conjugates, containing as a ligand tyrosine-o-sulfate in addition to one of the above mentioned oligosaccharides, were the most potent synthetic blockers. Compared with the most potent of the known inhibitors, fucoidan, bi-ligand glycoconjugate HSO3Lea-PAA-sTyr, displayed in vitro similar activity in blocking L-selectin, while its activity towards P-selectin was ten times lower. All the synthetic polymers tested were able to inhibit neutrophil extravasation to inflammation site, acting in concentration about 10 mg/kg. Thus, the effect of SiaLex is considerably more effective in vivo than in vitro, whereas heavily charged fucoidan and bi-ligand neoglycoconjugate acted in converse manner.
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PMID:[Inhibitory activity of monomeric and polymeric selectin ligands]. 1063 31

The aim of this work was to develop a calcium phosphate cement (CPC) providing controlled release of the antibiotic gentamicin sulfate (GS) over at least 1 week. The CPC was made of beta-tricalcium phosphate [beta-TCP; beta-Ca(3)(PO(4))(2)], monocalcium phosphate monohydrate [MCPM; Ca(H(2)PO(4))(2). H(2)O] and water. Release of GS was controlled by admixture of poly(acrylic acid) (PAA). The effects on the GS release kinetics of the molecular weight of PAA, of the amount of admixed PAA, and of the pH of the release medium were investigated. A typical cement sample weighed 3.6 g and contained 100 mg of GS and between 0 and 150 mg of PAA. In the following, PAA content is expressed as the weight ratio, lambda, with respect to GS. At a low PAA content in the CPC (lambda < 0.7), GS was released over 1-2 days according to a square-root-of-time kinetics, but not all GS was released. The unreleased GS fraction increased from 0 to 58% with an increase of PAA content (up to lambda = 0.7). At high PAA content (lambda > 0.7), GS was released over a period of up to 8 days according to a combination of a square-root-of-time and a zero-order kinetics. The total GS fraction released increased again from 58 to 100% with an increase of the amount of PAA (up to lambda = 1.5). These observations were explained by molecular interaction between PAA and GS resulting in gel formation. The maximum fraction of GS released from the cement was indeed a function of the solubility of the PAA-GS (coacervate) complex in the release medium. Thus, GS release was controlled by two mechanisms: (1) diffusion of free GS molecules through the porous cement (square-root-of-time kinetics); and (2) dissociation of GS from the PAA-GS complex (zero-order kinetics). The first mechanism was predominant at low lambda, whereas the second mechanism became important at high lambda and later release times. As the solubility of the PAA-GS complex decreased with an increase in PAA molecular weight, the higher molecular weight PAA yielded more prolonged release periods of up to 8 days. Interestingly, the use of 450 kDa PAA at lambda = 1.00 provided an almost constant release profile over a period of 7 days. Gel formation between PAA and GS was explained in terms of hydrogen bonding of PAA carboxyl groups with GS amino groups. The molar ratio between carboxyl groups and amino groups in the gel was estimated to be approximately 1.9. In conclusion, admixture of PAA into calcium phosphate cement appeared to be a very elegant tool to control the release of the antibiotic over a period of 7 to 8 days.
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PMID:Control of gentamicin release from a calcium phosphate cement by admixed poly(acrylic acid). 1098 May 1

P-selectin blocking potency was investigated using synthetic monomeric and polymeric anionic compounds containing sulfate groups such as O-sulfotyrosine (sTyr) and/or sulfated Lewis structures. A non-carbohydrate-containing polyacrylamide conjugate sTyr-PAA (80% mol of sTyr) was a remarkably potent inhibitor of P-selectin binding in vitro, having an IC(50) value of 6 ng/mL (equivalent to 10 nM calculated on the basis of sTyr residues or 0.1 nM calculated by the mass of the macromolecule). The inhibitory effect of sTyr-PAA (80%) towards P-selectin is significantly greater than that of fucoidan (IC(50), 100 ng/mL). However, sTyr-PAA (80%) was less effective than fucoidan at reducing neutrophil extravasation in an in vivo rat model of peritonitis.
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PMID:P-selectin blocking potency of multimeric tyrosine sulfates in vitro and in vivo. 1272 47


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