ABSTRACT
ß-Blockers and calcium channel blockers are commonly used drugs in the treatment of atrial fibrillation with tachycardia. However, in patients with high myocardial susceptibility and vulnerability, combination therapy with ß-blockers and non-dihydropyridine calcium channel blockers (verapamil or diltiazem) but also individual administration can cause drug-induced cardiogenic shock. Thus, the simultaneous administration of ß-blockers and non-dihydropyridine calcium channel blockers is absolutely contraindicated. In case of acute heart failure, isolated application is also contraindicated. In the treatment of a cardiogenic shock induced by ß-blockers and/or non-dihydropyridine calcium channel blockers, administration of intravenous calcium, glucagon or high-dose insulin is recommended.
Subject(s)
Atrial Fibrillation/drug therapy , Carbazoles/adverse effects , Carbazoles/therapeutic use , Critical Care/methods , Propanolamines/adverse effects , Propanolamines/therapeutic use , Shock, Cardiogenic/chemically induced , Tachycardia/drug therapy , Verapamil/adverse effects , Verapamil/therapeutic use , Aged, 80 and over , Carvedilol , Drug Interactions , Drug Therapy, Combination , Female , Humans , Infusions, IntravenousABSTRACT
The interaction of ruminant IgG with human phagocytes was assessed using Fc receptor (FcR)-mediated ingestion and the triggering of a respiratory burst as effector functions indicative of receptor-specific interaction. In monomeric form, ruminant IgG was three to five orders of magnitude less potent than homologous IgG in inhibiting FcR-specific phagocytosis by monocytes. However, when attached to tanned sheep erythrocytes (Es-T), ruminant IgG was opsonic, as it promoted enhanced phagocytosis of Es-T, comparable to ingestion of rabbit IgG-coated Es. This phagocytosis was inhibitable by high concentrations of human IgG in the fluid phase. Moreover, Es-T precoated with ferritin could be opsonized to a similar degree by anti-ferritin IgG from rabbit and cow. However, only bovine IgG1, but not IgG2, was opsonic. Bovine and goat IgG of some, but not other, suppliers were inactive. Similar results were obtained by measuring the respiratory burst triggered by heat-aggregated IgG, using a luminol-enhanced chemiluminescence assay. Thus, human IgG and ruminant IgG stimulated monocytes and, to a lesser extent, polymorphonuclear leucocytes (PMN), to generate CL. Depending on the manufacturer, some preparations of bovine and goat IgG were inactive, and bovine IgG2 failed to induce CL. These findings prove that certain ruminant IgG preparations, including bovine IgG1 interacting weakly with homologous PMN and monocytes, do interact with human PMN, monocytes and macrophages in a FcR-specific manner when offered in complexed form. Inhibition studies suggest that bovine IgG1 interacts mainly with human FcR type II. In contrast, bovine IgG2, regarded as cytophilic for homologous PMN, fails to interact with human PMN, monocytes and macrophages.
Subject(s)
Immunoglobulin G/metabolism , Phagocytes/immunology , Receptors, Fc/metabolism , Receptors, IgG/metabolism , Animals , Binding, Competitive , Cattle , Cells, Cultured , Respiratory Burst , Sheep , Species SpecificityABSTRACT
A modified ELISA for the detection of S. aureus strains producing toxic shock syndrome toxin (TSST-1) is described. Polystyrene balls are coated with specific sheep antibody and incubated with an over-night culture of suspected colonies. Biotinylated second antibody and an Avidin/biotinylated enzyme system are used to obtain an easily readable qualitative reaction.
Subject(s)
Bacterial Toxins , Enterotoxins/analysis , Enzyme-Linked Immunosorbent Assay , Shock, Septic/diagnosis , Staphylococcal Infections/diagnosis , Staphylococcus aureus/isolation & purification , Superantigens , Enterotoxins/biosynthesis , Humans , Staphylococcus aureus/metabolismABSTRACT
A modified ELISA for the detection of toxic shock syndrome toxin (TSST-1) from staphylococcal isolates is described. It displayed 100% correlation with the procedure based on isoelectric focusing and microslide precipitation. Commercially available immunoglobulins exhibited high antitoxin titres and it is suggested that they be used therapeutically.
Subject(s)
Bacterial Toxins , Enterotoxins/analysis , Staphylococcus aureus/analysis , Superantigens , Antibodies/immunology , Enterotoxins/immunology , Enzyme-Linked Immunosorbent Assay , Humans , gamma-Globulins/immunology , gamma-Globulins/therapeutic useABSTRACT
High doses of intravenous immunoglobulin were given to seven pregnant women between the 27th and 36th wk of gestation who were at risk for preterm delivery. Determinations of IgG subclasses and of antibodies against group B streptococcal serotypes, pneumococcal polysaccharides, and tetanus toxoid were done in maternal serum before and after intravenous IgG infusion and after delivery in cord serum. Substantial transplacental passage of the infused material could be observed in five cases where delivery occurred at the 34th wk or later. After the 36th wk of gestation, IgG subclass and antibody concentrations in cord serum were increased up to the levels in the maternal serum.
Subject(s)
Immunoglobulin G/analysis , Infant, Newborn/immunology , Maternal-Fetal Exchange , Streptococcus agalactiae/immunology , Streptococcus pneumoniae/immunology , Tetanus Toxoid/immunology , Antibodies/analysis , Female , Gestational Age , Humans , Immunoglobulin G/administration & dosage , Infusions, Parenteral , PregnancySubject(s)
Bacteria/genetics , Biological Evolution , Selection, Genetic , Viruses/genetics , Animals , Gene Frequency , Humans , MutationSubject(s)
Antigens, Surface/analysis , Bacterial Toxins , Cattle Diseases/diagnosis , Escherichia coli Infections/veterinary , Escherichia coli/immunology , Feces/immunology , Fimbriae, Bacterial/immunology , Animals , Cattle , Enzyme-Linked Immunosorbent Assay , Escherichia coli Infections/diagnosisABSTRACT
We compared four versions of the enzyme-linked immunosorbent assay for their suitability for detecting staphylococcal enterotoxins. The sandwich with labeled antibody proved to be the best. We used it with a sorbent consisting of antibody-coated polystyrene spheres reacted with 20 ml of food extract. The sensitivity of the test was 0.1 ng of enterotoxin per ml, which is far below clinical relevance. The succinimidyl-pyridyl-dithio-propionate enzyme coupling method of Pharmacia was superior to the two-step glutaraldehyde technique. Interfering protein A was eliminated by the simple addition of normal rabbit serum to the extracts. A diagnostic kit is now available.
Subject(s)
Enterotoxins/analysis , Enzyme-Linked Immunosorbent Assay , Immunoenzyme Techniques , Staphylococcus aureus , Evaluation Studies as TopicABSTRACT
Horse IgE was isolated from a serum pool collected from foals naturally infected with endoparasites. The serum was precipitated with ammonium sulfate, delipidated with dextran sulfate and further purified by gel filtration, anionic exchange, immunosorption or preparative polyacrylamide gelelectrophoresis. By these methods IgE could be isolated at a purity of 81%. The sera from rabbits immunized with the purified horse serum fractions were tested using reversed passive cutaneous anaphylaxis and an enzyme linked immunosorbent assay (ELISA). By the ELISA method cross reaction of rabbit anti horse IgE sera to human, mouse and rat myeloma IgE was demonstrated. Rat myeloma IgE also served to monitor the production of antibodies to horse IgE in rabbits.
Subject(s)
Horses/immunology , Immunoglobulin E/isolation & purification , Animals , Chromatography , Electrophoresis, Polyacrylamide Gel , Enzyme-Linked Immunosorbent AssayABSTRACT
An enzyme-linked immuno sorbent assay (ELISA) for measuring horse IgE specific to ovalbumin, bencylpenicilloic acid and odinitrocarboxyphenol is described. We used a sandwich type of ELISA by which horse serum was incubated in antigen-coated tubes containing one additional polystyrene ball, followed by rabbit anti horse IgE serum. The tubes were then incubated with biotinylated goat anti rabbit globulin followed by avidin coupled to phosphatase. Endpoint titrations were compared. The ELISA is highly reproducible due to the pretreatment of the polystyrene with glutaraldehyde. The increased antigen surface area led to a higher sensitivity of the test. The assay can be easily modified for the measurement of other Ig classes and of IgE of other antigen specificities.
Subject(s)
Enzyme-Linked Immunosorbent Assay , Horses/immunology , Immunoenzyme Techniques , Immunoglobulin E/immunology , AnimalsABSTRACT
Rabbit antisera against soluble human milk galactosyltransferase (GT) having anti-GT activity, as demonstrated by inhibition of enzyme activity were used for a comparative study of the molecular sizes of galactosyltransferase. For this purpose, affinity-purified antibodies were used for the identification of milk, serum and effusion galactosyltransferase from native or partially purified preparations resolved by sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE) by the immune replica technique. Milk galactosyltransferase migrated as a 55-kilodalton (kD) protein, serum and effusion GT slightly faster. Cross-reactive enzyme forms of 110 kD and 20 kD were detected in milk only. In order to establish a relationship between intracellular and soluble galactosyltransferase, HeLa cells were metabolically labeled by [35S]-methionine, cells lysed, subjected to immunoprecipitation and the precipitate analyzed by SDS-PAGE/fluorography: a single band corresponding to the intracellular form of GT have similar mobility as the milk enzyme was detected. These results indicate a close structural similarity between soluble and cellular galactosyltransferase as judged by immunological cross-reactivity and electrophoretic mobility.
Subject(s)
Lactose Synthase/analysis , Animals , Ascitic Fluid/enzymology , Electrophoresis, Polyacrylamide Gel , Female , HeLa Cells/enzymology , Humans , Lactose Synthase/blood , Lactose Synthase/immunology , Milk/enzymology , Molecular WeightABSTRACT
An enzyme-linked immunosorbent assay (ELISA) was adapted for the serological differential diagnosis of cystic or alveolar echinococcosis in man caused by Echinococcus granulosus or E. multilocularis respectively. By affinity chromatography using rabbit anti hydatid fluid IgG coupled covalently to CNBr-Sepharose 4B a protein fraction (Em 1) containing shared antigens of both parasites could be isolated from an extract of E. multilocularis metacestode tissue. From the same source another antigen fraction (Em 2) with a high degree of specificity for E. multilocularis was prepared by immunosorption. Antigen Em 1 was equally sensitive for the detection of antibodies against E. granulosus and E. multilocularis, whereas antigen fraction Em 2 appeared to be more specific for E. multilocularis. A correct serological differential diagnosis was achieved in 95% of 57 confirmed cases of human cystic or alveolar echinococcosis by the simultaneous use of both antigen fractions in the ELISA and by comparison of their reactivities.
Subject(s)
Antibodies/analysis , Antigens/analysis , Echinococcosis/diagnosis , Echinococcus/immunology , Animals , Antigens/isolation & purification , Echinococcosis/etiology , Enzyme-Linked Immunosorbent Assay , Epitopes , Humans , Isoelectric Focusing , RabbitsABSTRACT
Monospecific rabbit anti-human milk galactosyltransferase antibodies were used to develop a solid-phase enzyme-linked immunosorbent assay (ELISA) for the human milk enzyme. The assay was based on competition with galactosyltransferase-phosphatase conjugate. The detection limit of the standard curve was 30 ng/ml. Galactosyltransferase was quantified in dialyzed milk samples by ELISA with variation coefficients of less than 7.7% and between 6.8 and 18.8% within and between assays, respectively. The average content was 61 +/- 19 microgram/ml. The assay proved suitable for quantitation of partially purified enzyme preparations in body fluids.