RESUMEN
A hospital-managed project for the advanced care of children in their homes (SABH) has been established in Sweden. The aim was to provide an alternative to inpatient paediatric care by providing hospital-at-home care to stable infants and children using mobile units based on advanced information and communication technology. The Karolinska Hospital children's ward and emergency room referred children to SABH care. A medical care plan was drawn up by the physicians and nurses responsible for the patient while in hospital, in conjunction with the parents and the patient. In one year, 350 episodes of care requiring 3000 bed-days were managed by SABH in the children's homes rather than at hospital. Forty-two per cent of the patients were aged less than one year, 41% were between one and six years old, and 17% were older than six years. SABH care was at least 30% cheaper than conventional hospital care and patient satisfaction with the service was high. At the conclusion of the two-year project, the SABH became a permanent unit at the Karolinska Hospital.
Asunto(s)
Servicios de Atención a Domicilio Provisto por Hospital/organización & administración , Planificación de Atención al Paciente/organización & administración , Telemedicina/organización & administración , Cuidadores , Niño , Preescolar , Análisis Costo-Beneficio , Episodio de Atención , Humanos , Lactante , Recién Nacido , Satisfacción del Paciente , Relaciones Profesional-Familia , Garantía de la Calidad de Atención de Salud , Programas Informáticos , Suecia , Telemetría/instrumentaciónRESUMEN
Chlorite dismutase has been purified from the chlorate-metabolizing bacterium Ideonella dechloratans. The purified enzyme is tetrameric, with a relative molecular mass of 25,000 for the subunit, and contains about 0.6 heme/subunit as isolated. Its catalytic properties are similar, but not identical, to those found for a similar enzyme purified earlier from the bacterium GR-1. The heme group in Ideonella chlorite dismutase is readily reduced by dithionite, in contrast to the GR-1 enzyme, and redox titration gave a value of -21 mV for the midpoint potential at pH 7. The heme group has been characterized by optical and EPR spectroscopy. It is high-spin ferric at neutral pH, with spectroscopic properties similar to those found for cytochrome c peroxidase. In the alkaline pH range, a low-spin compound is formed. A 22-residue N-terminal amino acid sequence has been determined and no homologue has been found in the protein sequence databases.