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Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Poly-gamma-glutamic acid (gamma-PGA) obtained from Bacillus licheniformis ATCC 9945 was evaluated as a potential biosorbent material for use in the removal of heavy metals from aqueous solution. Copper (Cu(2+)) was chosen as the model heavy metal used in these studies since it is extensively used by electroplating and other industries, has been the model for many other similar studies, and can be easily assayed through a number of convenient methods. Cu(2+)-gamma-PGA binding parameters under varying conditions of pH, temperature, ionic strength, and in the presence of other heavy metal ions were determined for the purified biopolymer using a specially designed dialysis apparatus. Applying the Langmuir adsorption isotherm model showed that gamma-PGA had a copper capacity approaching 77.9 mg/g and a binding constant of 32 mg/L (0.5 mM) at pH 4.0 and 25 degrees C. Cu(2+)-gamma-PGA adsorption was relatively temperature independent between 7 and 40 degrees C, while an increase in ionic strength led to a decrease in metal ion binding. Cd(2+) and Zn(2+) ions compete with Cu(2+) for binding sites on the gamma-PGA biopolymer. Metal uptake by gamma-PGA was further tested using a tangential flow filtration apparatus in a diafiltration mode in which metal was continually processed through a dilute solution of gamma-PGA without allowing for equilibrium to be established. The circulating polymer solution was able to complex metal as well as successfully prevent passage of unbound copper ions present in solution through the membrane. Using 500 mL of a 0.2% gamma-PGA solution, up to 97% of a 50 mg/L copper sulfate solution processed at a flow rate of 115 mL/min was retained by the polymer. For a 10 mg/L solution of Cu(2+) as copper sulfate, filtrate concentrations of Cu(2+) never rose above 0.6 mg/L while processing 2.5 L of dilute copper sulfate.
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PMID:A heavy metal biotrap for wastewater remediation using poly-gamma-glutamic acid. 1659 72

Two pepsins (A and B) were purified from the stomach of pectoral rattail (Coryphaenoides pectoralis) by acidification, ammonium sulfate precipitation, gel filtration chromatography and anion exchange chromatography to obtain a single band on native-PAGE and SDS-PAGE. The purities of pepsin A and B were increased to 7.1- and 13.0-fold with approximately 5.7% and 2.2% yield, respectively. Pepsin A and B had the apparent molecular weights of 35 and 31 kDa, respectively, when analyzed using SDS-PAGE and Sephacryl S-200 gel filtration. Pepsin A and B showed maximal activity at pH 3.0 and 3.5, respectively, and had the same optimal temperature at 45 degrees C using hemoglobin as a substrate. Both pepsin A and B were stable in the pH range of 2.0-6.0 but were unstable at the temperatures greater than 40 degrees C. Activity of both pepsins was inhibited by pepstatin A and was activated by divalent cations, indicating pepsin characteristics. Activities of both pepsins continuously decreased as NaCl concentration increased (0-30%). The enzymes had high affinity and activity toward hemoglobin with Km and Kcat values of 98-152 microM and 32-50 S(-1), respectively. Purified pepsins generally showed the similar characteristics to other fish pepsins.
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PMID:Purification and characterization of two pepsins from the stomach of pectoral rattail (Coryphaenoides pectoralis). 1749 57

Newly synthesized vanadyl-poly(gamma-glutamic acid) complex (VO-gamma-PGA) with a VO(O4) coordination mode was found to have potent antidiabetic activity in streptozotocin (STZ)-induced type 1 diabetic mice (STZ-mice), compared with that of a solution containing only vanadyl sulfate, VOSO4. This was the first example of orally active vanadyl complex of gamma-PGA for treating STZ-mice. To better define its efficacy, we examined here the effects of VO-gamma-PGA treatment in STZ-mice by oral administration at the dose of 10 mg V/kg body mass for a longer period time than our previous study. The improvement in diabetic states in STZ-mice compared with saline-treated nondiabetic normal Std ddY mice. It was found that the elevated blood glucose levels in STZ-mice significantly decreased after 3 days and sustained the normalized blood glucose level around 180-200 mg/dL (10-11.1 mM) for the last 14 days, which is close to the blood glucose levels 100-200 mg/dL (5.6-11.1 mM) in nondiabetic normal Std ddY mice. The improvement in diabetes was strongly corelated by the improvement in oral glucose tolerance ability, glycosylated hemoglobin (HbA1c) levels and blood pressure, and serum parameters. The present results confirmed that VO-gamma-PGA complex is a promising, orally active insulin-mimetic agent to treat type 1 diabetic mice.
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PMID:Antidiabetic activity of the orally effective vanadyl-poly (gamma-glutamic acid) complex in streptozotocin(STZ)-induced type 1 diabetic mice. 1749 57

The periodontopathogen Aggregatibacter actinomycetemcomitans forms tenacious biofilms on abiotic surfaces in vitro. The objective of the present study was to measure the susceptibility of A. actinomycetemcomitans biofilms to detachment and killing by the anionic surfactant sodium dodecyl sulfate (SDS). We found that biofilms formed by a wild-type strain were resistant to detachment by SDS. In contrast, biofilms formed by an isogenic mutant strain that was deficient in the production of PGA (poly-N-acetyl-glucosamine), a biofilm matrix polysaccharide, were sensitive to detachment by SDS. Pre-treatment of wild-type biofilms with dispersin B, a PGA-degrading enzyme, rendered them sensitive to detachment by SDS and resulted in a > 99% increase in SDS-mediated cell killing. We concluded that PGA protects A. actinomycetemcomitans cells from detachment and killing by SDS. Dispersin B and SDS may be useful agents for treating chronic infections caused by A. actinomycetemcomitans and other PGA-producing bacteria.
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PMID:Detachment and killing of Aggregatibacter actinomycetemcomitans biofilms by dispersin B and SDS. 1758 7

The naturally occurring edible biopolymer poly(gamma-glutamic acid) (gamma-PGA) is shown to be an efficient chelating agent of vanadium(IV). The structure of poly(gamma-glutamic acid)oxovanadium(IV) (VO-gamma-PGA) complex in solution has been analyzed by electron spin resonance and UV-visible absorption spectra. The equatorial coordination sphere of vanadium(IV) is proposed to be [2 x carboxylate (2O)-VO-(OH2)2]. The binding isotherm is determined for suspensions of gamma-PGA in vanadium(IV) oxide sulfate (VS) solutions of different concentrations, and the data have been adjusted to fit the modified Langmuir equation. The maximum amount of vanadium bound per gram of gamma-PGA is estimated to be 141 mmol . g(-1) with a binding constant of 22 L . g(-1) at pH 3.
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PMID:Chelation of vanadium(IV) by a natural and edible biopolymer poly(gamma-glutamic acid) in aqueous solution: structure and binding constant of complex. 1794 Nov 10

Pepsin from the stomach of albacore tuna, skipjack tuna, and tongol tuna was characterized. Pepsin from all tuna species showed maximal activity at pH 2.0 and 50 degrees C when hemoglobin was used as a substrate. Among the stomach extract of all species tested, that of albacore tuna showed the highest activity (40.55 units/g tissue) (P < 0.05). Substrate-Native-PAGE revealed that pepsin from albacore tuna and tongol tuna consisted of 2 isoforms, whereas pepsin from skipjack tuna had only 1 form. The activity was completely inhibited by pepstatin A, while EDTA (ethylenediaminetetraacetic acid), SBTI (soybean trypsin inhibitor), and E-64 (1-(L-trans-epoxysuccinyl-leucylamino)-4-guanidinobutane) exhibited negligible effect. The activity was strongly inhibited by SDS (sodium dodecyl sulfate) (0.05% to 0.1%, w/v). Cysteine (5 to 50 mM) also showed an inhibitory effect in a concentration dependent manner. ATP, molybdate, NaCl, MgCl(2), and CaCl(2) had no impact on the activity. When tuna pepsin (10 units/g defatted skin) was used for collagen extraction from the skin of threadfin bream for 12 h, the yield of collagen increased by 1.84- to 2.32-fold and albacore pepsin showed the comparable extraction efficacy to porcine pepsin. The yield generally increased with increasing extraction time (P < 0.05). All collagen obtained with the aid of tuna pepsin showed similar protein patterns compared with those found in acid-solubilized collagen. Nevertheless, pepsin from skipjack tuna caused the degradation of alpha and beta components. All collagens were classified as type I with large portion of beta-chain. However, proteins with molecular weight (MW) greater than 200 kDa were abundant in acid-solubilized collagen.
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PMID:Tuna pepsin: characteristics and its use for collagen extraction from the skin of threadfin bream (Nemipterus spp.). 1857 87

The development of blended biomacromolecule and polyester scaffolds can potentially be used in many tissue engineering applications. This study was to develop a poly(gamma-glutamic acid)-graft-chondroitin sulfate-blend-poly(epsilon-caprolactone) (gamma-PGA-g-CS/PCL) composite biomaterial as a scaffold for cartilage tissue engineering. Chondroitin sulfate (CS) was grafted to gamma-PGA, forming a gamma-PGA-g-CS copolymer with 1-ethyl-3-(3-dimethyl-aminopropyl) carbodiimide (EDC) system. The gamma-PGA-g-CS copolymers were then blended with PCL to yield a porous gamma-PGA-g-CS/PCL scaffold by salt leaching. These blended scaffolds were characterized by (1)H NMR, ESCA, water-binding capacity, mechanical test, degradation rate and CS assay. The results showed that with gamma-PGA-g-CS as a component, the water-binding capacity and the degradation rate of the scaffolds would substantially increase. During a 4 week period of culture, the mechanical stability of gamma-PGA-g-CS/PCL scaffolds was raised gradually and chondrocytes were induced to function normally in vitro. Furthermore, a larger amount of secreted GAGs was present in the gamma-PGA-g-CS/PCL matrices than in the control (PCL), as revealed by Alcian blue staining of the histochemical sections. Thus, gamma-PGA-g-CS/PCL matrices exhibit excellent biodegradation and biocompatibility for chondrocytes and have potential in tissue engineering as temporary substitutes for articular cartilage regeneration.
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PMID:Fabrication and characterization of poly(gamma-glutamic acid)-graft-chondroitin sulfate/polycaprolactone porous scaffolds for cartilage tissue engineering. 1928 62

Maize (Zea mays) endosperm ADP-glucose pyrophosphorylase (AGPase) is a highly regulated enzyme that catalyzes the rate-limiting step in starch biosynthesis. Although the structure of the heterotetrameric maize endosperm AGPase remains unsolved, structures of a nonnative, low-activity form of the potato tuber (Solanum tuberosum) AGPase (small subunit homotetramer) reported previously by others revealed that several sulfate ions bind to each enzyme. These sites are also believed to interact with allosteric regulators such as inorganic phosphate and 3-phosphoglycerate (3-PGA). Several arginine (Arg) side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding. Alanine-scanning mutagenesis was applied to the corresponding Arg residues in both the small and large subunits of maize endosperm AGPase to determine their roles in allosteric regulation and thermal stability. Steady-state kinetic and regulatory parameters were measured for each mutant. All of the Arg mutants examined--in both the small and large subunits--bound 3-PGA more weakly than the wild type (A(50) increased by 3.5- to 20-fold). By contrast, the binding of two other maize AGPase allosteric activators (fructose-6-phosphate and glucose-6-phosphate) did not always mimic the changes observed for 3-PGA. In fact, compared to 3-PGA, fructose-6-phosphate is a more efficient activator in two of the Arg mutants. Phosphate binding was also affected by Arg substitutions. The combined data support a model for the binding interactions associated with 3-PGA in which allosteric activators and inorganic phosphate compete directly.
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PMID:Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase. 1988 75

Microbially produced gamma-polyglutamic acid (gamma-PGA) is a commercially important biopolymer with many applications in biopharmaceutical, food, cosmetic and waste-water treatment industries. Owing to its increasing demand in various industries, production of gamma-PGA is well documented in the literature, however very few methods have been reported for its recovery. In this paper, we report a novel method for the selective recovery and purification of gamma-PGA from cell-free fermentation broth of Bacillus licheniformis. The cell-free fermentation broth was treated with divalent copper ions, resulting in the precipitation of gamma-PGA, which was collected as a pellet by centrifugation. The pellet was resolubilized and dialyzed against de-ionized water to obtain the purified gamma-PGA biopolymer. The efficiency and selectivity of gamma-PGA recovery was compared with ethanol precipitation method. We found that 85% of the original gamma-PGA content in the broth was recovered by copper sulfate-induced precipitation, compared to 82% recovery by ethanol precipitation method. Since ethanol is a commonly used solvent for protein precipitation, the purity of gamma-PGA precipitate was analyzed by measuring proteins that co-precipitated with gamma-PGA. Of the total proteins present in the broth, 48% proteins were found to be co-precipitated with gamma-PGA by ethanol precipitation, whereas in copper sulfate-induced precipitation, only 3% of proteins were detected in the final purified gamma-PGA, suggesting that copper sulfate-induced precipitation offers better selectivity than ethanol precipitation method. Total metal content analysis of the purified gamma-PGA revealed the undetectable amount of copper ions, whereas other metal ions detected were in low concentration range. The purified gamma-PGA was characterized using infrared spectroscopy.
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PMID:A novel Method for the selective recovery and purification of gamma-polyglutamic acid from Bacillus licheniformis fermentation broth. 2006 85

Poly-gamma-glutamic acid (gamma-PGA) prepared by fermentation of microbe was used as drug carrier for vanadium sulfate to obtain vanadyl-poly-gamma-glutamic acid (VO-gamma-PGA) complex. The FI-IR spectrum of the complex demonstrated that the expected VO-gamma-PGA complex is formed by the coordination of VO(2+) through the side chain carboxylic groups of the gamma-PGA. Studies of the complex in treating type I diabetes were carried out on alloxan induced diabetes rats. The results of treating the rats in 2 weeks and then stopping administration for 10 days showed that VO-gamma-PGA can effectively lower blood glucose levels of diabetic rats during administration. But after ceasing treatment there were no differences between groups in blood glucose level and water intake. The results of oral glucose tolerance and some serum parameters also demonstrated that VO-gamma-PGA was more effective than vanadium sulfate in treating diabetic rats.
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PMID:Effects of insulin-mimetic vanadyl-poly(gamma-glutamic acid) complex on diabetic rat model. 2012 19


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