PubMed · 8808018
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
C M Wyman. 1996-02-01. Preventing medication errors.. https://doi.org/10.1093/ajhp%2F53.3.257
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Serving medical needs aboard deployed Navy ships presents unique challenges. One of these is selecting agents for treating a myocardial infarction at sea. After comparing the currently available thrombolytic agents with respect to ease of administration, efficacy, storage requirements, cost, antigenicity, and other complications, we believe that streptokinase best meets the need for a thrombolytic agent aboard Navy ships. If associated antithrombotic therapy with heparin is considered necessary, then subcutaneous administration may often be preferred to intravenous use for reasons of cost and simplicity.
The storage requirements for parenteral products vary with the characteristics of the medication in the product. Temperature, light, moisture, pH, composition of the container, type of infusion fluid, and exposure to other chemical substances are the major determinants of the stability of parenteral medication stored in the patient's home.
PURPOSE: Protein aggregates are thought to be involved in the immunogenicity of recombinant proteins in humans. To probe human IFN-alpha formulations for the presence of soluble protein aggregates, enzyme-linked immunosorbent assays (ELISA) were developed. METHODS: For the detection of IFN-alpha-IFN-alpha and HSA-IFN-alpha aggregates, sandwich ELISAs were developed using a monoclonal anti-IFN-alpha antibody as a capture antibody and the same anti-IFN-alpha antibody and an anti-human serum albumin (HSA) antibody (HRP-labeled), respectively. RESULTS: Marketed freeze-dried, HSA-containing IFN-alpha-formulations tested in the ELISAs all contained IFN-alpha-IFN-alpha and/or HSA-IFN-alpha protein aggregates, although in varying amounts. These aggregates were predominantly IFN-alpha dimers and 1:1 conjugates of HSA with IFN-alpha. Test formulations revealed that aggregation of IFN-alpha was strongly affected by the presence of pharmaceutical excipients, pH of the formulation, lyophilisation procedure, and storage temperature and time. CONCLUSIONS: The ELISAs are rapid, highly specific for aggregates in the presence of both IFN-alpha and HSA monomers and allow the direct detection of both types of aggregates in formulations in the nanogram range. The new assays will assist the monitoring of the aggregate-inducing processes during IFN-alpha formulation and storage in an early phase and the development of aggregate-free IFN-alpha formulations.