ABSTRACT
Positioning of the dispersive electrode has no significant effect during radiofrequency ablation. Doubling the surface are of the dispersive electrode results in a lower impedance, higher current delivery, and increased tip temperatures, particularly if the baseline impedance is >100 ohms. These findings may have important implications for optimizing radiofrequency energy delivery using currently available radiofrequency generators.
Subject(s)
Catheter Ablation/instrumentation , Electrodes , Cardiac Catheterization/instrumentation , Catheter Ablation/methods , Cohort Studies , Electric Conductivity , Electric Impedance , Equipment Design , Female , Humans , Male , Middle Aged , Surface Properties , Temperature , ThermometersSubject(s)
Arboviruses/immunology , Immune Sera , Animals , Chromatography, Gel , Guinea Pigs , Hemagglutination , UltracentrifugationSubject(s)
Blood , Respiratory Syncytial Viruses/drug effects , Viruses , Animals , Antibodies/analysis , Antiviral Agents/analysis , Antiviral Agents/pharmacology , Cattle , Chemical Precipitation , Chromatography, Gel , HeLa Cells , Hemagglutination Inhibition Tests , Mercaptoethanol/pharmacology , Neutralization Tests , Orthomyxoviridae/drug effects , Respirovirus/immunology , Swine , Trypsin/pharmacology , gamma-Globulins/analysisABSTRACT
1. Immunosorbents were prepared by coupling activated aminocellulose with the gamma-globulin concentrates of antisera prepared against ovalbumin and human serum albumin. 2. The immunosorbents were low in solubility, but high in capacity for homologous antigens. 3. The high specificity of these immunosorbents was demonstrated by their use in fractionating various mixtures of fluorescent ovalbumin, (131)I-labelled human serum albumin, lysozyme and ribonuclease.
ABSTRACT
1. gamma-Globulin concentrates of antisera prepared against ovalbumin and human serum albumin were thiolated and cross-linked to form insoluble polymers. 2. These immunosorbents were of low solubility and of high capacity for homologous antigen. 3. The high specificity of these immunosorbents was demonstrated by fractionation of various binary mixtures of fluorescent ovalbumin, (131)I-labelled human serum albumin, lysozyme and ribonuclease.
