salicylates and Hemolysis

Interactions of salicylates with the hematopoietic system are reviewed. Development of anemia is discussed with respect to fluid retention, gastrointestinal bleeding, and hemolytic anemia. Alterations in polymorphonuclear leukocyte and platelet function are evaluated. Interactions with anticoagulants and with the coagulation system are identified.

Topics: Aspirin; Blood Platelets; Gastrointestinal Hemorrhage; Hematologic Diseases; Hematopoietic System; Hemolysis; Hemostasis; Humans; Leukocytes; Salicylates

Topics: Androgens; Anesthetics; Animals; Biological Transport; Carboxyhemoglobin; Cats; Cobalt; Cyanates; Dogs; Fentanyl; Haplorhini; Hemoglobins; Hemolysis; Humans; In Vitro Techniques; Methemoglobinemia; Methylene Blue; Oxygen Consumption; Phosphates; Prednisone; Propranolol; Rats; Salicylates

Topics: Anemia; Anemia, Hypochromic; Anemia, Macrocytic; Anemia, Sideroblastic; Arthritis, Rheumatoid; Erythrocyte Count; Folic Acid Deficiency; Gastrointestinal Hemorrhage; Hemolysis; Humans; Iron; Plasma Volume; Salicylates; Vitamin B 12 Deficiency

Topics: Abnormalities, Drug-Induced; Anti-Bacterial Agents; Anticoagulants; Antimetabolites; Antineoplastic Agents; Antithyroid Agents; Female; Fetal Diseases; Fetus; Hemolysis; Hormones; Humans; Infant, Newborn; Infant, Newborn, Diseases; Maternal-Fetal Exchange; Pregnancy; Reserpine; Salicylates; Thalidomide; Tolbutamide; Vitamin K

A series of novel salicylic acid derivatives containing metronidazole as Staphylococcus aureus Tyrosyl-tRNA synthetase (TyrRS) inhibitors have been synthesized and evaluated their biology activities as potential antibacterial agents. Among these compounds, compound 5r exhibited the most potent antibacterial activity against Gram-positive (S. aureus ATCC 6538 and Bacillus subtilis ATCC 6633) and Gram-negative (Escherichia coli ATCC 35218 and Pseudomonas aeruginosa ATCC 13525) with MICs of 0.39-1.57 μg/mL and showed the most potent S. aureus Tyrosyl-tRNA synthetase inhibitory with 2.3 μM. Docking simulation was performed to insert compound 5r into the crystal structure of S. aureus Tyrosyl-tRNA synthetase active site to determine the probable binding model. These results suggested that compound 5r may be a promising antibacterial agent.

Topics: Anti-Infective Agents; Binding Sites; Crystallography, X-Ray; Drug Design; Erythrocytes; Gram-Negative Bacteria; Gram-Positive Bacteria; Hemolysis; Humans; Metronidazole; Microbial Sensitivity Tests; Molecular Conformation; Molecular Docking Simulation; Protein Structure, Tertiary; Salicylates; Staphylococcus aureus; Structure-Activity Relationship; Tyrosine-tRNA Ligase

We have recently designed and developed a dual-functional drug carrier that is based on poly(ethylene glycol) (PEG)-derivatized farnesylthiosalicylate (FTS, a nontoxic Ras antagonist). PEG5K-FTS2 readily form micelles (20-30 nm) and hydrophobic drugs such as paclitaxel (PTX) could be effectively loaded into these micelles. PTX formulated in PEG5K-FTS2 micelles showed an antitumor activity that was more efficacious than Taxol in a syngeneic mouse model of breast cancer (4T1.2). In order to further improve our PEG-FTS micellar system, four PEG-FTS conjugates were developed that vary in the molecular weight of PEG (PEG2K vs PEG5K) and the molar ratio of PEG/FTS (1/2 vs 1/4) in the conjugates. These conjugates were characterized including CMC, drug loading capacity, stability, and their efficacy in delivery of anticancer drug PTX to tumor cells in vitro and in vivo. Our data showed that the conjugates with four FTS molecules were more effective than the conjugates with two molecules of FTS and that FTS conjugates with PEG5K were more effective than the counterparts with PEG2K in forming stable mixed micelles. PTX formulated in PEG5K-FTS4 micelles was the most effective formulation in inhibiting the tumor growth in vivo.

Topics: Animals; Breast Neoplasms; Disease Models, Animal; Drug Carriers; Farnesol; Female; HCT116 Cells; Hemolysis; Humans; Inhibitory Concentration 50; Magnetic Resonance Spectroscopy; Mammary Neoplasms, Experimental; MCF-7 Cells; Mice; Mice, Inbred BALB C; Micelles; Paclitaxel; Polyethylene Glycols; Salicylates

The use of herbal preparations for staunching blood flow and reducing the risk of vascular thrombosis is common worldwide. In this study, aqueous and methanolic extracts of plants used to treat blood-associated complaints were investigated to determine their effects on red blood cell haemolysis and coagulation. The extent of haemolysis was determined spectrophotometrically. Prothrombin time (PT) and activated partial thromboplastin time (aPTT) as indicators of coagulation rate were determined using a coagulatometer. All of the plant extracts tested had a significant effect on coagulation time, prolonging the aPTT. Cassia petersiana had the greatest prolonging effect on PT compared to the control, phosphate buffered saline (PBS). As all of the herbal extracts tested had a delaying effect on coagulation, patients using herbal/plant therapies should be cautioned to stop their medication before surgery.

Topics: Anticoagulants; Blood Coagulation; Chromatography, Thin Layer; Coumarins; Hemolysis; Herb-Drug Interactions; Humans; Medicine, African Traditional; Partial Thromboplastin Time; Plant Extracts; Plants, Medicinal; Prothrombin Time; Salicylates; South Africa; Species Specificity

Complement plays a vital role in both the innate and adaptive immune systems. It recognizes a target, opsonizes it, generates anaphylatoxins, and directly kills cells through the membrane attack complex (MAC). This final function, which assembles C5b-9(n) on viable cell surfaces, can kill host cells through bystander lysis. Here we identify for the first time compounds that can inhibit bystander lysis while not interfering with the other essential functions of complement. We show that aurin tricarboxylic acid (ATA), aurin quadracarboxylic acid (AQA), and aurin hexacarboxylic acid (AHA), block the addition of C9 to C5b-8 so that the MAC cannot form. These molecules inhibit hemolysis of human, rat, and mouse red cells with a half maximal inhibitory concentration (IC(50)) in the nanomolar range. When given orally to Alzheimer disease type B6SJL-Tg mice, they inhibit MAC formation in serum and improve memory retention. On autopsy, they show no evidence of harm to any organ. Aurin tricarboxylic acid, aurin quadracarboxylic acid, and aurin hexacarboxylic acid may be effective therapeutic agents in Alzheimer disease and other degenerative disorders where self damage from the MAC occurs.

Topics: Alzheimer Disease; Animals; Aurintricarboxylic Acid; Bystander Effect; Complement System Proteins; Hemolysis; Humans; Memory; Mice; Mice, Transgenic; Rats; Salicylates

We compared the COBAS(R) acetaminophen and salicylate assays (Roche Diagnostics) with the Stanbio GDS assays (Stanbio Laboratories) that are currently used in our laboratory with respect to interferences from hemolysis and lipemia.. Acetaminophen and salicylate were added into human serum with varying concentrations of hemoglobin or Intralipid to generate a range of acetaminophen and salicylate concentrations. Then the COBAS and GDS assays were used to measure the apparent drug concentrations; the H and L indices were measured to determine the extent of hemolysis and lipemia present in each specimen.. Both hemolysis and lipemia have less effect on the COBAS(R) acetaminophen and salicylate assays than on the GDS assays.. The COBAS assays for acetaminophen and salicylate are preferable to the current GDS assays in clinical toxicology laboratories.

Topics: Acetaminophen; Biological Assay; Hemolysis; Humans; Hyperlipidemias; Reproducibility of Results; Salicylates

The basic phospholipase A(2) (VRV-PL-VIIIa) from Vipera russelli venom induces multiple toxic effects including neurotoxicity, myotoxicity, edema and hemorrhage. This phospholipase A(2) has been extensively characterized for its pharmacological properties except for hemorrhagic activity. In the present investigation, the lung hemorrhagic activity was assayed using lung dye diffusion method. The investigations to understand the mechanism of lung hemorrhage induction by VRV-PL-VIIIa was followed by chemical modification studies and also by interaction with an antihemorrhagic factor p-anisic acid (4-methoxy benzoic acid). In presence of 1:2 mol:mol PLA(2): anisic acid, the lung hemorrhagic and edema inducing activities were completely neutralized in experimental animals; however, catalytic and anticoagulant activities were not neutralized. Carbamylation of VRV-PL-VIIIa resulted in the loss of lung hemorrhage and edema inducing activities. In contrast, carbamylation of VRV-PL-VIIIa in the presence of anisic acid could not neutralize the lung hemorrhage and edema inducing activities. The anticoagulant and enzyme activities were only partially neutralized when carbamylated both in the presence and absence of anisic acid.

Topics: Animals; Anticoagulants; Betaine; Carbamyl Phosphate; Daboia; Edema; Group II Phospholipases A2; Hemolysis; Hemorrhage; Hydroxybenzoate Ethers; Lung Diseases; Male; Mice; Phospholipases A; Proteins; Prothrombin Time; Rats; Salicylates; Spectrometry, Fluorescence; Viper Venoms

The hemolytic activity of dapsone is well known to reside in its N-hydroxylamine metabolites. Addition of dapsone hydroxylamine (DDS-NOH) to red cell suspensions causes damage such that when reintroduced into the circulation of isologous rats, the injured cells are rapidly removed by the spleen. Hemolytic activity is associated with the extensive formation of disulfide-linked hemoglobin adducts on red cell membrane skeletal proteins. To determine if free radicals could be involved in this process, rat red cells were incubated with DDS-NOH in the presence of the spin trap, 5,5'-dimethyl-1-pyrroline-N-oxide (DMPO) and subjected to EPR analysis. Addition of DDS-NOH (25-50 microM) to a red cell suspension gave rise to a four-line (1:2:2:1) EPR spectrum with coupling constants identical to those of a DMPO-hydroxyl radical adduct (DMPO-OH) standard. No other radicals were detected; however, preincubation of red cells with cysteamine caused the DDS-NOH-generated DMPO-OH signal to be replaced by a cysteamine thiyl radical adduct signal. DDS-NOH-treated red cells were also found to contain ferrylhemoglobin, indicating the presence of hydrogen peroxide. Furthermore, DDS-NOH was found to stimulate salicylate hydroxylation in red cell suspensions, confirming the presence of oxygen radicals. These data support the hypothesis that oxygen radicals are involved in the mechanism underlying dapsone-induced hemolytic anemia.

Topics: Animals; Cyclic N-Oxides; Cysteamine; Dapsone; Disulfides; Electron Spin Resonance Spectroscopy; Erythrocytes; Free Radicals; Glutathione; Hemoglobins; Hemolysis; Hydroxyl Radical; Hydroxylation; Male; Rats; Rats, Sprague-Dawley; Reactive Oxygen Species; Salicylates; Spin Labels

Topics: Antioxidants; Ascorbic Acid; Butylated Hydroxytoluene; Chromium; Erythrocytes; Hemoglobins; Hemolysis; Humans; Kinetics; Maleates; Oxidation-Reduction; Oxyhemoglobins; Salicylates; Salicylic Acid; Vitamin E

A novel enzymatic assay for salicylate in serum has been developed. Salicylate monooxygenase and NADH are used to convert the drug to catechol. This is reacted with 4-aminophenol at high pH to yield a blue product, which is detected colorimetrically. The assay is complete in less than seven minutes and requires no sophisticated equipment. The method is precise, sensitive and shows excellent accuracy in recovery experiments and when compared to a high performance liquid chromatography method. The assay is free from interference by coloured or turbid samples, salicylate metabolites, structurally related compounds such as benzoate and 4-hydroxybenzoate, and a range of drugs. The assay reagents demonstrate excellent stability. The formulation of the assay in two stages provides increased specificity and sensitivity compared to other emergency salicylate assays and allows the inclusion of reagents to greatly enhance the stability of the salicylate monooxygenase-NADH reagent, yet the method is simple and performs well.

Topics: Buffers; Catechols; Colorimetry; Hemolysis; Humans; Indicators and Reagents; Jaundice; Kinetics; Lipids; Mixed Function Oxygenases; NAD; Salicylates

The mechanism underlying uptake of certain compounds in ionized form across human red blood cell membrane was examined. The ionized forms of salicylate, 5-methoxy-salicylate and phenylalanylphenylalanine were significantly taken up into the interior space of human red blood cells instead of remaining in the membrane. Inhibition of the uptake of these compounds by 4,4'-diisothiocyano-2,2'-disulfonate stilbene and phlorizin indicates that their permeation of the erythrocyte membrane may involve the membrane protein fraction. Chelation at the protein site does not appear to occur. Instead, an amino group in the protein structure may mediate the transport of these ionized compounds.

Topics: Absorption; Biological Transport; Dipeptides; Erythrocyte Membrane; Hemolysis; Humans; Hydroxybenzoate Ethers; Hydroxybenzoates; In Vitro Techniques; Ions; Osmolar Concentration; Salicylates; Salicylic Acid

The haemolytic effect of methylsalicylate (MS) on human and sheep erythrocytes is reported for the first time to our knowledge. Human erythrocytes are more sensitive to this effect. Haemolysis is proportional to the concentration of methylsalicylate and the duration of incubation. Lowering of surface tension and the ensuing membrane damage appear to be the mechanism by which the haemolytic effect is produced.

Topics: Erythrocyte Membrane; Erythrocytes; Hemolysis; Humans; In Vitro Techniques; Membrane Lipids; Phospholipids; Salicylates; Sterols; Surface Tension

Topics: Acetazolamide; Adult; Animals; Erythrocyte Membrane; Erythrocytes; Hemolysis; Histamine; Humans; In Vitro Techniques; Male; Procaine; Salicylates; Sheep; Tetracycline; Urethane

Topics: 3',5'-Cyclic-AMP Phosphodiesterases; Analgesics; Animals; Anti-Inflammatory Agents; Anti-Inflammatory Agents, Non-Steroidal; Hemolysis; Male; Mice; Organophosphates; Organophosphorus Compounds; Platelet Aggregation; Prostaglandins; Rats; Salicylates; Stomach Ulcer

In the present study we examined the utility, sensitivity and specificity of the cadmium- and heat-induced hemolysis, investigating the effects of diclofenac, salicylate and lidocaine, carticaine and procaine on the rabbit erythrocyte membrane. In the cadmium-induced hemolysis, which has not been reported, as far as we know, as a test model for local anesthetics, the studied local anesthetics have, to a large extent, protective effects on the erythrocyte membranes, probably based on an osmotic action at drug concentrations of 10(-4) to 10(-2) M. On the other hand, these local anesthetics amplify the heat-induced hemolysis to a variable extent. The studied antirheumatic drugs showed in the cadmium-induced hemolysis that they cannot have the same binding sites as the local anesthetics investigated. In the cadmium-induced hemolysis, the reaction products of the antirheumatic drugs with the membrane protein presumably cannot cause an increase in surface area/volume ratio of the erythrocytes, which is generally regarded as a cause for stabilization. This interpretation could be an explanation for the increase of the cadmium-induced hemolysis by the antirheumatic drugs studied. On the other hand, the antirheumatic drugs inhibited to a variable extent the heat-induced hemolysis.

Topics: Anesthetics, Local; Animals; Anti-Inflammatory Agents; Cadmium; Carticaine; Diclofenac; Dose-Response Relationship, Drug; Hemolysis; Hot Temperature; Hydrogen-Ion Concentration; In Vitro Techniques; Lidocaine; Procaine; Rabbits; Salicylates

Evidence from the literature indicates that in vitamin E-deficient animals prostaglandin (PG) synthesis in platelets is enhanced while it is decreased in the muscle and testis. In the present study the effects of aspirin, a known inhibitor of PG biosynthesis, on vitamin E deficiency signs in the rat were investigated. Administration of aspirin to vitamin E-deficient rats had no protective effect on fetal mortality, incisor depigmentation, body weight gain or red blood cell peroxidative hemolysis. Aspirin prevented the anemia and thrombocythemia observed in vitamin E-deficient rats. Aspirin, salicylic acid and a carbazole prostaglandin inhibitor exacerbated testis degeneration in vitamin E-deficient animals. Addition of aspirin to the diet more than doubled the vitamin E requirement for reversal of necrotizing myopathy.

Topics: Animals; Aspirin; Blood Cell Count; Female; Fetal Death; Hematocrit; Hemoglobins; Hemolysis; Male; Pregnancy; Pregnancy Complications; Prostaglandins; Rats; Salicylates; Testis; Vitamin E Deficiency

A boy, 2 years old, developed a HUS after a pneumonitis. He was treated with Heparin, salicylates and recurrent peritoneal dialysis and recovered slowly. The course of the disease was complicated by myocarditis, gastric hemorrhage and severe neurologic disturbances. 7 days after unset of hemolysis a cold agglutinin titer of 1:256 was detected. This fact arises the question whether infection with Mycoplasma pneumoniae and the presence of cold agglutinins in serum could be involved in the development of HUS. The possibility of a viral etiology for this disease is discussed.

Topics: Agglutinins; Child, Preschool; Cold Temperature; Gastrointestinal Hemorrhage; Hemolysis; Hemolytic-Uremic Syndrome; Heparin; Humans; Lung Diseases; Male; Mycoplasma Infections; Myocarditis; Nervous System Diseases; Peritoneal Dialysis; Salicylates

The binding of salicylic acid and sulfathiazole to bovine whole blood, plasma proteins, and purified albumin fraction was investigated using a dynamic dialysis system. The binding profiles for salicylic acid were quite similar in bovine plasma and 4% bovine serum albumin. In contrast, the binding of sulfathiazole was significantly greater in the plasma than in solutions of fraction V bovine serum albumin. Data from dynamic dialysis binding studies of the compounds, conducted in whole blood and suspended erythrocyte systems, did not lend themselves to analysis by classical methods. Hemolysis and alteration in the nature of the protein binding sites during the binding studies were shown to be factors that could explain the unusual binding observed in the whole blood system.

Topics: Animals; Binding Sites; Binding, Competitive; Cattle; Erythrocytes; Hemolysis; In Vitro Techniques; Plasma; Protein Binding; Salicylates; Serum Albumin, Bovine; Sulfathiazoles; Time Factors

Salicylate is known to uncouple mitochondrial oxidative phosphorylation. Since the viability of pyruvate-kinase-deficient reticulocytes depends on ATP generated by mitochondrial metabolism, this study examined the effects of salicylate on erythrocytes deficient in pyruvate kinase. When deficient erythrocytes from patients with severe hemolysis were incubated with salicylate (2 to 30 mg per deciliter), there was a marked decrease (25 to 75 percent) in ATP. In addition, this drug-induced ATP depletion produced cell potassium and water loss, and the normal oxidant responsiveness of the hexose-monophosphate shunt was blunted. Since these cellular abnormalities are associated with accelerated hemolysis in vivo, the data suggest that aspirin therapy may aggravate hemolysis in patients with pyruvate kinase deficiency whose erythrocyte manifest sensitivity to salicylate in vitro.

Topics: Adenosine Triphosphate; Anemia, Hemolytic; Aspirin; Erythrocytes; Glucose; Glucosephosphate Dehydrogenase Deficiency; Hemolysis; Hexoses; Humans; Mitochondria; Oxidative Phosphorylation; Pyruvate Kinase; Salicylates

Most work on human erythrocyte interaction with drugs and other compounds has been reported on the basis of total concentrations. Total concentrations alone do not reveal numbers of molecules bound per cell, v. This paper emphasizes determination of v and of binding isotherms, in conjunction with changes in cell morphologies and in hypotonic shock behavior as v is varied. Four drugs and five other compounds were studied, with fresh erythrocytes. The principal findings are: (1) the intact erythrocyte engages in two kinds of binding mechanisms, statistical binding and cooperative binding, depending on the compound. In the case of a detergent, dodecylbenzene sulfonate, the binding is nearly quantitative. (2) The compounds often induce considerable protection against hypotonic hemolysis. However, the binding levels at which maximum protection occurs are rather close to the levels, vL, that occur upon complete conversion to the first distorted morphology. Therefore, the maximally protected erythrocyte may be a distorted erythrocyte. (3) The value n is the apparent total number of sites from Scatchard plotting for compounds which bind in a statistical manner. Levels vp and vw characterize maxima in cooperative binding behavior, also from Scatchard plotting of the data. Despite the wide diversity of over-all levels at which compounds exert their effects, the critical binding levels of and numbers of sites fall into a narrow range:n, vL, vP, and vw are all between 1 and 8 times 10-7 molecules or sites per cell. Most of our data, and that from some other laboratories, indicate that about 2 plus and minus 1 times 10-7 sites per erythrocyte are available for compound binding by the intact cell. Beyond that level, the cell in suspension almost always will be forced into the first obvious morphology change, as seen by phase contrast microscopy. (4) Once stoichiometries are established, the total binding capacity of erythrocytes for such compounds, in blood, can be estimated. An intruding organic molecule would encounter about 6 times as many plasma albumin sites as erythrocyte sites, if the plasma albumin sites were free. However, because albumin in vivo usually forms a complex with one to two fatty acids, the erythrocyte itself is rather likely to act as a transport particle for such compounds.

Topics: Binding Sites; Chlorpromazine; Erythrocytes; Hemolysis; Humans; Kinetics; Mathematics; Methylene Blue; Microscopy, Phase-Contrast; Osmolar Concentration; Phenanthrenes; Propranolol; Quinine; Salicylates

For studies on the lysosome-stabilizing effect of D-glucaric acid derivatives which have been found to have anti-inflammatory effect, the available and soluble enzyme activities of acid phosphatase of rat liver lysosomes were determined. Saliployed as standards. Lysosomes were incubated with drugs under specific conditions which allowed the data on the stabilizing activity of the drugs to be reproducible. The inhibitory effect of D-glucaro-1, 4-lactone, salicylic acid and phenylbutazone onover a wide range of concentrations. D-glucaro-1, 4-lactone as well as salicylic acid exhibited concentration-dependent lysosome-stabilizing effect whereas phenlybutazone had an optimum concentration for its lysosome-stabilizing effect. In addition, D-glucaro-1, 4-lactone,saliclicacid and phenylubtazone were also examined for their effects on heat-induced and saponin-induced hemolysis of rat erythrocyres. Both salicylic acid and phenylbutazone exhibited potent stabilziing and labilizing effects on heat-induced and saponin-induced hemolysis of eryhthrocytes, respectively. D-glucaro-1, 4-lactone, however, was incabale of affecting the hemolysis of erythrocytes. There appears to be a difference in the mechanism of the lysosome-stabilizing effects between D-glucaric acid derivatives and other anti-inflammatory drugs.

Topics: Acid Phosphatase; Adipates; Animals; Anti-Inflammatory Agents; Dose-Response Relationship, Drug; Erythrocytes; Ethanol; Hemolysis; In Vitro Techniques; Liver; Lysosomes; Male; Monosaccharides; Phenylbutazone; Rats; Salicylates; Saponins; Sucrose; Sugar Acids

Topics: Amino Acids; Autoanalysis; Azides; Bilirubin; Buffers; Drug Storage; Hemolysis; Humans; Indicators and Reagents; Lipoprotein Lipase; Methods; Photometry; Salicylates; Spectrophotometry, Ultraviolet; Temperature; Urea

Theobromine sodium salicylate exerts an inhibitory effect on lysis of rabbit red cells by streptolysin O. No similar action of related compounds has been demonstrated.

Topics: Animals; Caffeine; Erythrocytes; Hemolysis; In Vitro Techniques; Rabbits; Salicylates; Streptolysins; Theobromine; Theophylline

Topics: Anilides; Anthracenes; Buffers; Cell Membrane; Erythrocytes; Hemolysis; Humans; Hydrogen-Ion Concentration; Methods; Osmotic Fragility; Phenothiazines; Photolysis; Porphyrins; Radiation Effects; Salicylates; Solvents; Spectrophotometry; Sulfonamides; Tetracycline; Ultraviolet Rays

Topics: Anilides; Chromatography, Thin Layer; Evaluation Studies as Topic; Hemolysis; Humans; Hydrogen-Ion Concentration; Methods; Osmotic Fragility; Photolysis; Radiation Effects; Salicylates; Spectrum Analysis; Ultraviolet Rays

Topics: Animals; Antigen-Antibody Reactions; Caseins; Complement Fixation Tests; Complement System Proteins; Depression, Chemical; Edetic Acid; Hemagglutination Tests; Hemolysis; Heparin; Humans; Kinetics; Oximes; Phlorhizin; Salicylates; Sheep

Topics: Animals; Anti-Inflammatory Agents; Aspirin; Betamethasone; Capillary Permeability; Chloroquine; Dogs; Erythrocytes; Female; Flufenamic Acid; Guinea Pigs; Hemolysis; Lipid Metabolism; Lipids; Mefenamic Acid; Oxyphenbutazone; Peroxides; Phenylbutazone; Prednisolone; Radiation Effects; Salicylates; Ultraviolet Rays

Topics: Animals; Anti-Inflammatory Agents; Aspirin; Betamethasone; Cell Membrane; Chloroquine; Dogs; Erythrocytes; Flufenamic Acid; Hemolysis; Humans; In Vitro Techniques; Lipid Metabolism; Mefenamic Acid; Oxyphenbutazone; Peroxides; Phenylbutazone; Prednisolone; Salicylates

Topics: Aminopyrine; Animals; Anti-Inflammatory Agents; Aspirin; Blood Coagulation; Cell Membrane; Dogs; Erythrocytes; Flufenamic Acid; Hemolysis; Hot Temperature; Hydrogen-Ion Concentration; Indomethacin; Lysophosphatidylcholines; Nitrobenzenes; ortho-Aminobenzoates; Oxyphenbutazone; Phenylbutazone; Phospholipases; Protein Denaturation; Pyrazoles; Salicylates; Saponins; Serum Albumin, Bovine; Sulfates; Surface-Active Agents

Topics: Adult; Bromides; Calcium Chloride; Citrates; Dimethyl Sulfoxide; Erythrocytes; Glucose; Glycols; Hemolysis; Humans; In Vitro Techniques; Iodides; Lactose; Male; Polyethylenes; Potassium; Propylene Glycols; Salicylates; Sodium; Sodium Chloride; Solutions; Water

Topics: Animals; Cattle; Dextrans; Dialysis; Erythrocytes; Guinea Pigs; Hemagglutination; Hemolysis; Horses; Humans; Polyvinyls; Povidone; Rabbits; Salicylates; Sheep; Urea

Topics: Anaphylaxis; Animals; Anti-Allergic Agents; Antigen-Antibody Reactions; Antirheumatic Agents; Detergents; Erythrocytes; Guinea Pigs; Hemolysis; Pharmacology; Phenylbutazone; Precipitin Tests; Research; Salicylates; Serum Albumin; Sheep; Sheep, Domestic; Sulfates

Topics: Animals; Crotalid Venoms; Cysteine; Ecchymosis; Formaldehyde; Glucuronates; Guanidine; Guanidines; Hemolysis; Injections, Intraperitoneal; Injections, Subcutaneous; Lagomorpha; Mice; Pharmacology; Rabbits; Research; Salicylates; Snake Venoms; Snakes; Sulfates; Thioglycolates; Toxicology; Trimeresurus; Urea; Venoms

Topics: Anesthetics; Anesthetics, Local; Benzoates; Hemolysis; Humans; Isotonic Solutions; Phenmetrazine; Procaine; Salicylates; Sodium Chloride

Topics: Aldehydes; Cell Death; Hemolysis; Oximes; Salicylates

Topics: Hemolysis; Humans; Salicylates; Sodium Salicylate; Urea