1,107 research outputs found
Experimental tests about the cooling/freezing of the molten salts in the receiver tubes of a solar power plant with parabolic trough
No full textIn 2003 ENEA realized the PCS experimental Facility at Casaccia Research Centre (Rome, Italy), in order to test in real operating conditions the components of a parabolic trough solar plant, and to evaluate the technical feasibility of using the solar molten salts mixture (60% NaNO3, 40% KNO3, melting point 220÷240°C) in such a type of plant. ENEA also had the need to assess the behaviour of the solar receiver tubes during abnormal operating situations (wrong operation, pump block, power failure, etc.), when a block of the circulation of the molten salts may occur and cause the cooling or, worse, the freezing of the salts mixture inside the pipes. Some experimental tests have been performed, aimed to examine what happens in such a cases. In fact, without quick maneuvers to restart the circulation of the molten salts or to readily empty the receiver tubes, the molten salts contained in them may cool down to temperatures near/below the solidification. In this report are shown the results of the experimental tests carried out on the receiver tubes of the PCS Facility by cooling the process fluid down to temperatures near or below its freezing point. The tests show that the solidification of the salts does not damage the components of the plant but it is manageable and reversible, provided you apply the correct procedures. © 2017 Author(s)
Expression of L-ornithine Ndelta-oxygenase (PvdA) in fluorescent Pseudomonas species: an immunochemical and in silico study
No full textPeroxynitrite Detoxification by Human Haptoglobin:Hemoglobin Complexes: A Comparative Study.
No full textHaptoglobin (Hp) reacts with dimeric hemoglobin (Hb), shifts the equilibrium in favor of the αβ dimer and displays heme-based catalysis. Here, kinetics of peroxynitrite scavenging by ferric human haptoglobin1-1:hemoglobin and haptoglobin2-2:hemoglobin complexes (Hp1-1:Hb(III) and Hp2-2:Hb(III), respectively) is reported between pH 6.2 and 8.3 at 20.0 °C. The reactivity of Hp1-1:Hb(III) and Hp2-2:Hb(III) against peroxynitrite is similar to that of tetrameric Hb(III), reflecting the R-like structure of the αβ dimers of Hb(III) bound to Hp. To investigate the protective role of Hp1-1:Hb(III) and Hp2-2:Hb(III) against peroxynitrite-mediated nitration, the relative yield of nitro-l-tyrosine formed by the reaction of peroxynitrite with free l-tyrosine was determined. Interestingly, both Hp1-1:Hb(III) and Hp2-2:Hb(III) impair peroxynitrite-mediated nitration of free l-tyrosine. Therefore, Hp:Hb complexes could participate to the detoxification of reactive nitrogen and oxygen species in vivo, contributing to prevent extra-erythrocytic Hb-induced damage during hemolytic crisis
Pseudo-enzymatic hydrolysis of 4-nitrophenyl myristate by human serum albumin.
No full textMost of the esterase properties of human serum albumin (HSA) are the result of multiple irreversible chemical modifications rather than turnover. The HSA-catalyzed hydrolysis of 4-nitrophenyl myristate (NphOMy) is consistent with the minimum three-step mechanism involving the acyl-enzyme intermediate HSA-OMy: Under all the experimental conditions, values of K(s) (= k(-1)/k(+1)), k(+2), and k(+2)/K(s) determined under conditions where [HSA]⩾5×[NphOMy] and [NphOMy]⩾5×[HSA] match very well each other. The deacylation process is rate limiting in catalysis (i.e., k(+3)≪k(+2)) and k(-2)∼k(-3)∼0s(-1). The pH dependence of k(+2)/K(s), k(+2), and K(s) reflects the acidic pK(a)-shift of one ionizing group from 8.9±0.2 in NphOMy-free HSA to 6.8±0.3 in the HSA:NphOMy adduct. The HSA-catalyzed hydrolysis of NphOMy is inhibited competitively by diazepam, indicating that Tyr411 is the active-site nucleophile
Abacavir modulates peroxynitrite-mediated oxidation of ferrous nitrosylated human serum heme-albumin
No full textThe pH dependence of pre-steady-state and steady-state kinetics for the papain-catalyzed hydrolysis of N-alpha-carbobenzoxyglycine p-nitrophenyl ester
No full textPre-steady-state and steady-state kinetics of the papain (EC 3.4.22.2)-catalyzed hydrolysis of N-alpha-carbobenzoxyglycine p-nitrophenyl ester (ZGlyONp) have been determined between pH 3.0 and 9.5 (I = 0.1 M) at 21 +/- 0.5 degrees C. The results are consistent with the minimum three-step mechanism involving the acyl X enzyme intermediate E X P: (Formula: see text). The formation of the E X S complex may be regarded as a rapid pseudoequilibrium process; the minimum values for k+1 are 8.0 microM-1 s-1 (pH less than or equal to 3.5) and 0.40 microM-1 s-1 (pH greater than 6.0), and that for k-1 is 600 s-1 (pH independent). The pH profile of k+2/Ks (= kcat/Km; Ks = k-1/k+1) reflects the ionization of two groups with pK' values of 4.5 +/- 0.1 and 8.80 +/- 0.15 in the free enzyme. The pH dependence of k+2 and k+3 (measured only at pH values below neutrality) implicates one ionizing group in the acylation and deacylation step with pK'' values of 5.80 +/- 0.15 and 3.10 +/- 0.15, respectively. As expected from the pH dependences of k+2/Ks (= kcat/Km) and k+2, the value of Ks changes with pH from 7.5 X 10(1) microM (pH less than or equal to 3.5) to 1.5 X 10(3) microM (pH greater than 6.0). Values of k-2 and k-3 are close to zero over the whole pH range explored (3.0 to 9.5). The pH dependence of kinetic parameters indicates that at acid pH values (less than or equal to 3.5), the k+2 step is rate limiting in catalysis, whereas for pH values higher than 3.5, k+3 becomes rate limiting. The observed ionizations probably reflect the acid-base equilibria of residues involved in the catalytic diad of papain, His159-Cys25. Comparison with catalytic properties of ficins and bromelains suggests that the results reported here may be of general significance for cysteine proteinase catalyzed reactions
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