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PubMed · 491793

Computer-assisted patient-care management.

A Froment·P Michaud·H Milon·G Dechanoz·M Dupuy·R Magnon·S Melinon·C Bouveret·T Chorobik·H Falcoz
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Abstract

A computer-assisted patient-care management system is currently operating in two patient-care units as part of a pilot project at the Hôpital Cardiologique, a member institution of the Hospices Civils de Lyon. The system includes the management of administrative records (notice of admission set to the patient-care unit, appointment for admission sent to the patient, notice of admission set to the physician requesting hospitalization, admissions and discharges, patient census) and of patient-care records (orders, examinations, laboratory tests, medications, injections and treatments, a summary list or orders to be carried out during the day, labels for laboratory specimens and requistions for the tests and examinations to be performed); and the medical management of the patient (clinical summary of patient status at admission, results of tests and examinations, summary of hospitalization, data for research and statistics). Computerization was begun in 1977, following the implementation of individualized patient-care records in 1976. The system will be evaluated in 1978 and extended to the remainder of the hospital (18 patient-care units) by the end of 1979.

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A Froment, P Michaud, H Milon, G Dechanoz, M Dupuy, R Magnon, S Melinon, C Bouveret, T Chorobik, H Falcoz. Computer-assisted patient-care management.. https://doi.org/10.3109/14639237909003743

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PubMed1979

Purification and properties of hydrogenase from Megasphaera elsdenii.

A hydrogenase has been purified to homogeneity from the soluble fraction of the rumen bacterium Megasphaera elsdenii, the overall purification is 200 times with a yield of 14%. The pure enzyme consists of a single polypeptide chain with Mr approximately 50 000 which contains 12 atoms of non-haem iron and 12 atoms of acid-labile sulphide. The enzyme is rapidly inactivated by O2 and it is therefore purified under nitrogen and in the presence of sodium dithionite. The optical spectrum of the enzyme, after removal of the dithionite with air, shows a peak at 275 nm (epsilon 275 nm = 143 mM-1 cm-1) and a shoulder between 350 nm and 400 nm (epsilon 400 nm = 46 mM-1 cm-1). The enzyme catalyses hydrogen production from sodium dithionite at a low rate. The rate is greatly enhanced by addition of the electron donors flavodoxin, ferredoxin and methyl viologen. The kinetic data with these three electron donors suggest co-operativity, but no indication of self-association of the enzyme was obtained. Sodium chloride enhances the rate of hydrogen production with methyl viologen semiquinone and changes the kinetic behaviour of the enzyme with this electron donor, but causes inhibition of the reactions mediated by ferredoxin and flavodoxin. Two kinetic models were developed which are consistent with the kinetic data of the three electron donors tested. The apparent co-operativity for the hydrogen production can be fitted with the mathematical form of those models. The identical kinetic behaviour of the hydrogenase with the one-electron donors flavodoxin and methyl viologen semiquinone monomer and the two-electron donor ferredoxin indicates that the hydrogenase accepts two electrons in two separate, independent steps and further indicates that the two (4Fe-4S) clusters of the donor ferredoxin are independent. The interpretation of the kinetic data with methyl viologen semiquinone is complicated by the fact that the semiquinone dimerises, and that the formation of the dimer is enhanced by salt. Taking into account the association of this donor, the activity of the enzyme with methyl viologen semiquinone can be described by the sum of the activities of the enzyme with methyl viologen monomer and methyl viologen dimer. The enzyme catalyses the oxidation of hydrogen gas with methyl and benzyl viologen as electron acceptors to their semiquinone forms; both electron acceptors show Michaelis-Menten kinetics. The hydrogen oxidation activity with both electron acceptors is stimulated by addition of sodium chloride. The kinetic data of the oxidation of hydrogen with the two-electron acceptors used are consistent with the porposed models, if it is assumed that the pathway followed is compulsory. At this moment no choice can be made between the models proposed.

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