Introduction: The number of elderly patients in home care in France is currently increasing. Our objective is to describe the clinical characteristics, the care professionals' intervention and the complexity of follow-up care for this elderly population.
Methods: This is a cross-sectional study with a sample of 50 elderly patients aged 75 and over living at home and followed-up in home hospitalization in 2016 by the Assistance Publique Hôpitaux de Paris.
Introduction: In France, self-administration is less common for intramuscular (IM) than parenteral injections, because of the widespread availability of home visits by nurses, who can give these IM injections. An easy, personalized training program was set up to help French patients who wanted to be self-sufficient regarding their injections.
Methods: This noncomparative, open-label, multicenter study enrolled patients aged 18-75 years, diagnosed with relapsing-remitting multiple sclerosis (MS), with at least 2 relapses during the previous 3 years, no evidence of progression between relapses, and treated with IM interferon beta-1a.
Introduction: Psychological troubles are common in multiple sclerosis but their underlying etiology is still controversial.
Methods: The objective of this open, non comparative, multicenter study was to assess changes in global psychological functioning in new multiple sclerosis patients during the first 3 months of treatment with intramuscular interferon beta-1a once weekly (Avonex). This functioning was rated every 4 weeks with the GAF (Global Assessment Functioning) scale.
The time-resolved fluorescence emissions of the lone tryptophan residues in rat alpha-fetoprotein (RFP) and rat serum albumin (RSA) were studied. The total fluorescence intensity decays in both proteins were multiexponential. Analysis of the data by nonlinear least squares as a sum of discrete exponentials showed that four exponentials were needed for a satisfactory fit for both proteins.
View Article and Find Full Text PDFRat fetal serum alpha 1-fetoprotein (AFP), a heterogeneous glycoprotein, binds estrogens with high affinity but at a fractional number of sites even after treatment with charcoal (n = 0.6), which may mean 60% of the protein has 1 site and the remainder none. To investigate the origin of this fractional number of sites the "native" protein (purified by negative affinity chromatography) was further purified (step 1) and fractionated (step 2) into its two main charge variants (electrophoretically "slow" and "fast") by a two-step fast-protein liquid chromatography method.
View Article and Find Full Text PDF