Ingegerd Simonsson

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Risks and other uncertainties can cause losses, which lead to increasing costs and time delays,<lb>both during the project and at the end. The need to prevent failures during the construction<lb>process and other losses related to construction has been emphasised in various reports.<lb>Example consequences are failure costs in civil works which can be close(More)
A mechanism model has been presented that can describe most known kinetic properties of carbonic anhydrase isoenzymes I, II, and III. The essential features of this model include: Nucleophilic attack of metal-bound OH- on CO2 to form metal-bound HCO-3. Formation of metal-bound OH- from metal-bound H2O. In isoenzyme II, and probably also in isoenzyme I, this(More)
The effects of human carbonic anhydrase C on the 13C nuclear magnetic resonance spectra of equilibrium mixtures of 13CO2 and NaH13CO3 were measured at 67.89 MHz. Enzyme-catalyzed CO2-HCO-3 exchange rates were estimated from the linewidths of the resonances. The results show that: (a) the maximal exchange rates are larger than the maximal turnover rates; (b)(More)
The inhibition of human carbonic anhydrase II (carbonate hydro-lyase, EC 4.2.1.1) by tetrazole, 1,2,4-triazole, 2-nitrophenol, and chloral hydrate has been investigated. These inhibitors, together with phenol which has been studied previously (Simonsson, I., Jonsson, B.-H. and Lindskog, S. (1982) Biochem. Biophys. Res. Commun. 108, 1406-1412), can be(More)
Five monovalent anions, I-, N3-, SCN-, NCO- and Au(CN)2-, were investigated as inhibitors of CO2 hydration catalyzed by human carbonic anhydrase II (carbonate hydro-lyase, EC 4.2.1.1). Predominantly uncompetitive inhibition patterns were observed at pH near 9 in all cases. While Dixon plots of Km/V vs. inhibitor concentration were linear, all the(More)
Rates of CO2/HCO-3 exchange, catalyzed by human carbonic anhydrase I (or B) at chemical equilibrium, were estimated from the nuclear magnetic resonance linewidths of 13C-labeled substrates. The results show that the maximal exchange rate constant is independent of pH in the range 5.7-8.0, whereas the apparent substrate dissociation constant depends on pH.(More)
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