acid-phosphatase and Tuberculosis

Topics: Acid Phosphatase; Air Pollution; Animals; Asbestos; Chemical Phenomena; Chemistry; Cyclic N-Oxides; Glucuronidase; Humans; Hydrogen; L-Lactate Dehydrogenase; Lysosomes; Macrophages; Microscopy, Electron; Mycobacterium tuberculosis; Polyvinyls; Pulmonary Alveoli; Pyridines; Silicon Dioxide; Silicosis; Tuberculosis

Topics: Acid Phosphatase; Animals; Esterases; Hydrolases; Hypersensitivity, Delayed; Immunity; Macrophages; Peptide Hydrolases; Rabbits; Species Specificity; Tuberculosis

Objective To study the role of Rab7 in the blockage of autophagosome-lysosome fusion induced by secretory acid phosphatase (SapM), a virulence factor of mycobacterium tuberculosis. Methods The Raw264.7 cells were transfected with siRab7, and the P62 was detected using Western blotting. After transfected with mCherry-SapM, the co-localization of SapM and Rab7 in Raw264.7 cells was detected by immunofluorescence cytochemistry and the interaction of SapM with Rab7 was determined by co-immunoprecipitation. SapM mutants including SapM(δ ARCA), SapM(δ FRED) and SapM(δ CT) were used to transfect Raw264.7 cells, and their associations with Rab7 were analyzed. Results The treatment of siRab7 induced a significant increase of P62 in these cells. Immunofluorescence cytochemistry showed the intracellular co-localization of SapM and Rab7. Co-immunoprecipitation showed that SapM and Rab7 were precipitated by each other. Only SapM(δ CT) failed to interact with Rab7 among the three SapM mutants. Conclusion The inhibition of autophagosome-lysosome fusion induced by SapM is dependent on the interaction between SapM and Rab7.

Topics: Acid Phosphatase; Animals; Autophagosomes; Bacterial Proteins; Humans; Lysosomes; Macrophages; Mice; Mycobacterium tuberculosis; Protein Binding; rab GTP-Binding Proteins; rab7 GTP-Binding Proteins; RAW 264.7 Cells; Tuberculosis

Cathepsin K and tartrate-resistant acid phosphatase (TRAP) are two proteins expressed in osteoclastic giant cells. Recently we showed that lesional multinucleated giant cells (MNGs) in pulmonary granulomatosis with polyangiitis expressed these proteins. We aimed to clarify whether the expression of these two proteins has any specificity or is a general feature of MNGs associated with multiple types of granulomatous inflammation.. In total, 7 Crohn's disease (CD), 5 GCA, 5 giant cell myocarditis (GCM), 11 sarcoidosis and 6 tuberculosis cases were examined for expression of cathepsin K and TRAP using immunohistochemistry (IHC). Protein expression was semi-quantitatively classified as none, weak, moderate or strong. In addition, tissue TRAP activity was examined using an enzymatic reaction.. The expression of cathepsin K was robust in >95% of MNGs of all examined disease groups, whereas TRAP expression varied; CD, GCA and tuberculosis showed strong TRAP expression. TRAP expression in sarcoidosis and GCM was weaker (CD vs GCM, P = 0.04; CD vs sarcoidosis, P = 0.06). Compared with IHC, TRAP detection using an enzymatic colour reaction had limited sensitivity.. Expression of TRAP and cathepsin K is a general feature of MNGs and their expression might be related to histopathological pattern.

Topics: Acid Phosphatase; Biomarkers; Cathepsin K; Cells, Cultured; Crohn Disease; Giant Cells; Humans; Immunohistochemistry; Isoenzymes; Myocarditis; Osteoclasts; Paraffin Embedding; Sarcoidosis; Sensitivity and Specificity; Statistics, Nonparametric; Tartrate-Resistant Acid Phosphatase; Tuberculosis

Tuberculosis (TB) is responsible for nearly 1.4 million deaths globally every year and continues to remain a serious threat to human health. The problem is further complicated by the growing incidence of multidrug-resistant TB (MDR-TB) and extensively drug-resistant TB (XDR-TB), emphasizing the need for the development of new drugs against this disease. Phagosomal maturation arrest is an important strategy employed by Mycobacterium tuberculosis to evade the host immune system. Secretory acid phosphatase (SapM) of M.tuberculosis is known to dephosphorylate phosphotidylinositol 3-phosphate (PI3P) present on phagosomes. However, there have been divergent reports on the involvement of SapM in phagosomal maturation arrest in mycobacteria. This study was aimed at reascertaining the involvement of SapM in phagosomal maturation arrest in M.tuberculosis. Further, for the first time, we have also studied whether SapM is essential for the pathogenesis of M.tuberculosis. By deleting the sapM gene of M.tuberculosis, we demonstrate that MtbΔsapM is defective in the arrest of phagosomal maturation as well as for growth in human THP-1 macrophages. We further show that MtbΔsapM is severely attenuated for growth in the lungs and spleen of guinea pigs and has a significantly reduced ability to cause pathological damage in the host when compared with the parental strain. Also, the guinea pigs infected with MtbΔsapM exhibited a significantly enhanced survival when compared with M.tuberculosis infected animals. The importance of SapM in phagosomal maturation arrest as well as in the pathogenesis of M.tuberculosis establishes it as an attractive target for the development of new therapeutic molecules against tuberculosis.

Topics: Acid Phosphatase; Animals; Cell Line; Gene Deletion; Guinea Pigs; Humans; Macrophages; Mycobacterium tuberculosis; Phagosomes; Tuberculosis

It is established that isoniazid (isonicotinic acid hydrazide) can interact with A-I apolipoprotein to form a complex, which can be considered as the transport form of the preparation. The use of this complex for the treatment of mice with BCG-induced tuberculous inflammation led to an increase in the free activities of acid phosphatase and cathepsin D in the liver, which was decreased under the action of mycobacteria and the free form of isoniazid. The isoniazid complex with A-I apolipoprotein exhibited more expressed anti-inflammatory effect (estimated by the activity of chitotriosidase in blood serum) as compared to the free drug.

Topics: Acid Phosphatase; Animals; Antitubercular Agents; Apolipoprotein A-I; Cathepsin D; Drug Combinations; Hexosaminidases; Injections, Intraperitoneal; Isoniazid; Liver; Lysosomes; Male; Mice; Mice, Inbred CBA; Mycobacterium bovis; Tuberculosis; Up-Regulation

We studied the role of autochthonous microflora from body cavities in the development of tissue hypoxia and instability of cell membranes. In children with tuberculosis dysbiosis manifested in nonspecific quantitative changes in the intestinal microflora and the presence of coxsackievirus antigens in the urine. DNA-containing viruses with pronounced immunosuppressive activity (e.g., herpesvirus, measles virus, and rubella virus) were found in most children. Microbiological and virological changes were accompanied by the appearance of laboratory signs for tissue hypoxia, which included inhibition of Krebs cycle dehydrogenases and alpha-glycerophosphate pathway in blood lymphocytes. Regression analysis revealed a relationship between the content of extraintestinal coxsackieviruses and inactivation of alpha-glycerophosphate dehydrogenase, succinate dehydrogenase and ratio of facultatively anaerobic bacteria in microbiocenosis, and expression of acid phosphatase and total population of malonate-positive enterobacteria, staphylococci, yeasts, and enterococci.

Topics: Acid Phosphatase; Child; Child, Preschool; Enterobacteriaceae; Enterovirus; Glycerolphosphate Dehydrogenase; Humans; Hypoxia; Infant; Intestines; Lymphocytes; Tuberculosis; Urine

Live mycobacteria secrete a number of unique proteins early in their multiplication which are important for both the pathogenesis and the stimulation of specific host responses. We have investigated the mechanisms by which the host mounts immune response against tuberculosis after vaccination with secretory proteins (SP) of a vaccine candidate Mycobacterium habana TMC 5135. Mice vaccinated with SP of 10th day growth of M. habana, either alone or emulsified in Freund's incomplete adjuvant (FIA) possessed antituberculous resistance and cellular immune responses against M. tuberculosis H37Rv. These proteins induced a significant cutaneous delayed type hypersensitivity response in guinea pigs vaccinated with heat killed M. tuberculosis H37Rv, which was equivalent to that observed with a standard purified protein derivative (PPD). The splenocytes of these guinea pigs have shown higher proliferative response after stimulation with SP than with PPD. The SP + FIA immunization has been found to exert maximum prophylactic effect by potentiating both the oxygen dependent arms and enzymatic activities of macrophages. Macrophages from mice vaccinated with SP of M. habana produced enhanced levels of interleukin(IL)-2, interleukin-12 and interferon(IFN)-gamma. The protective as well as cell mediated immune responses were upregulated in SP immunized animals when compared to whole cell (M. habana) vaccinated animals. SDS-PAGE of SP from M. habana showed the prominent bands of 60, 32, 31 and 30 kDa. Furthermore, the western analysis of SP with pulmonary tuberculosis patient's serum has revealed the presence of immunoreactive antigens of 36, 35, 33/32 kDa. Overall study demonstrated that the secretory antigens released by actively growing M. habana bacilli could activate different arms of effective immune response.

Topics: Acid Phosphatase; Animals; Bacterial Proteins; Blotting, Western; Disease Models, Animal; Electrophoresis, Polyacrylamide Gel; Glucuronidase; Interferon-gamma; Interleukin-12; Interleukin-2; Mice; Mice, Inbred AKR; Muramidase; Mycobacterium; Reactive Oxygen Species; Tuberculosis

Tumour necrosis factor-alpha (TNF) plays a central role in the recruitment and activation of mononuclear cells in mycobacterial infection. In the absence of type 1 TNF receptor, Mycobacterium bovis Bacillus Calmette-Guerin (BCG) infection of mice is not contained, leading to fatal disease. Because type 1 TNF receptor binds both TNF and lymphotoxin-a, we used TNF-deficient mice to determine the specific role of TNF in the host resistance to BCG infection. The bacterial burden of the lungs of TNF-deficient mice was substantially increased and the mice succumbed to pneumonia between 8 and 12 weeks with a defective granuloma response. Atypical granulomas developed by 4 weeks expressing low levels of MHC class II, intracellular adhesion molecule (ICAM-1), CD11b and CD11c. Macrophages showed little signs of activation and had low levels of acid phosphatase activity and inducible nitric oxide synthase (INOS) expression. Despite the defective cellular recruitment, the chemokines, monocyte chemoattractant protein-1 (MCP-1) and macrophage inflammatory protein-1 (MIP-1alpha), were increased in broncho-alveolar lavage fluid of TNF-deficient mice. The defective host response was corrected by the transplantation of normal bone marrow cells into irradiated TNF-deficient mice. These results demonstrate that TNF derived from hemopoietic cells rather than from mesenchymal origin are essential for a normal host response to BCG infection. Furthermore, TNF dependent expression of adhesion molecules may be essential for the recruitment of mononuclear cells for the formation of bactericidal BCG granulomas.

Topics: Acid Phosphatase; Animals; Antigens, CD; Bone Marrow Transplantation; Granuloma; Histocompatibility Antigens Class II; Immunity, Innate; Integrin alphaXbeta2; Intercellular Adhesion Molecule-1; Lung; Macrophage-1 Antigen; Mice; Mice, Inbred C57BL; Mice, Knockout; Mycobacterium bovis; Pneumonia; Receptors, Tumor Necrosis Factor; Receptors, Tumor Necrosis Factor, Type I; Tuberculosis; Tumor Necrosis Factor-alpha

Rat peritoneal macrophages in vitro were infected with Mycobacterium tuberculosis and the fate of M. tuberculosis inside macrophages was monitored. Alteration in the levels of nitric oxide (NO) measured in terms of nitrite formed, hydrogen peroxide (H2O2) and lysosomal enzymes such as acid phosphatase, cathepsin-D and beta-glucuronidase in macrophages following M. tuberculosis infection was also studied. Elevation in the levels of nitrite were observed from 72 h of M. tuberculosis infection. Irrespective of the time point, M. tuberculosis infected macrophages produced elevated levels of H2O2. Maximum increase in the level of acid phosphatase was observed from 72 h of M. tuberculosis infection, whereas maximum elevation in the level of beta-glucuronidase was observed 48 h after M. tuberculosis infection. However these microbicidal agents did not alter the intracellular viability of M. tuberculosis.

Topics: Acid Phosphatase; Animals; Cathepsin D; Cells, Cultured; Glucuronidase; Hydrogen Peroxide; Macrophages, Peritoneal; Male; Mycobacterium tuberculosis; Nitric Oxide; Phagocytosis; Rats; Rats, Wistar; Tuberculosis

The studies of the effects produced by M. tuberculosis various strains on the activity of lysosomal enzymes in peritoneal mouse macrophages demonstrated multidirectional influence of the bacilli. Non-sedimentary activity rose in matrical enzymes indicating lysosomal membranes instability due to M. tuberculosis infection followed by hydrolase activation and hydrolases escape into the cytosol. An inhibiting action of pathogenic mycobacteria on lysosomal proteases is suggested.

Topics: Acid Phosphatase; Animals; beta-Galactosidase; beta-Glucosidase; Cathepsin D; Cathepsin E; Cathepsins; Enzyme Activation; Lysosomes; Macrophage Activation; Macrophages, Peritoneal; Male; Mice; Mycobacterium tuberculosis; Tuberculosis

The subcutaneous, intradermal, and pulmonary inflammatory lesions induced in mice by viable Mycobacterium bovis (BCG) with no glycolipid cord factor (CF) on the outer cell wall (delipidated BCG, dBCG) was drastically different from that induced by inoculation with intact bacteria. The reaction caused by dBCG was of an acute nature: the cells making up the inflammatory infiltrate exhibited polymorphonuclear-like (PMNs) morphologic characteristics, there was a decrease on delayed hypersensitivity response, and the lesion was resolved around the 16th day after inoculation. Complete disappearance of viable organisms from the lungs, liver, and spleen of these animals occurred in parallel with the dissipation of the dBCG-induced inflammatory infiltrate, showing that CF plays an important role in the host-parasite relationship that takes place in infections caused by mycobacteria. In addition, when deprived of this glycolipid component, bacilli lose their immunostimulant ability.

Topics: Acid Phosphatase; Animals; Cord Factors; Glycolipids; Hypersensitivity, Delayed; Immunization; Intradermal Tests; Lung; Macrophage Activation; Macrophages; Male; Mice; Mycobacterium bovis; Tuberculosis

A relation was sought between acid phosphatase contents and the presence of tubercle bacilli inside the peritoneal exudate cells (PEC) of normal guinea pigs and those immunized with BCG. This was done to investigate the role lysosomal enzymes play in the microbicidal capacity of the cell. In both normal and immune animals tubercle bacilli were present only in those PEC that contained acid phosphatase. Cells without acid phosphatase did not contain bacilli. Thus, only activated cells ingested bacilli. Under the conditions of these experiments, macrophage activation, as indicated by the presence of acid phosphatase, was not related to the immune status of the animal. Similarly, stimulation by ingestion of tubercle bacilli was not significant. Also, the number of acid phosphatase grains/cell did not influence the number of bacilli/cell. Thus, the acid phosphatase content of the cell did not correlate with the number of bacilli inside the cell. It was concluded that acid phosphatase may not be one of the factors that contribute to the microbicidal capacity of the cell.

Topics: Acid Phosphatase; Animals; Ascitic Fluid; BCG Vaccine; Guinea Pigs; Lysosomes; Macrophages; Mycobacterium tuberculosis; Phagocytosis; Tuberculosis

Topics: Acid Phosphatase; Animal Feed; Animals; Antibody-Producing Cells; Cattle; Chickens; Fossil Fuels; Immunity; Immunologic Techniques; Plasma Cells; Rats; Tuberculosis; Yeast, Dried

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Antibody-Producing Cells; Esterases; Guinea Pigs; Histocytochemistry; Lipase; Succinate Dehydrogenase; T-Lymphocytes; Thymus Gland; Tuberculosis

Topics: Acid Phosphatase; Animals; Cathepsins; Hydrogen-Ion Concentration; Macrophages; Mice; Mycobacterium tuberculosis; Peptide Fragments; Peptide Hydrolases; Peritoneum; Proteins; Pulmonary Alveoli; Tuberculosis

A patient with ectopic pinealoma first presented with apparent anorexia nervosa and hypernatraemic coma. A history of diabetes insipidus two months previously was not known on admission to hospital. The diabetes insipidus was unmasked by the administration of steroids. Neuroendocrinal and neuropathological aspects of the case are discussed with reference to the march of symptoms due to the growth of the tumour. Histochemical evidence is presented supporting the similarity between ectopic pinealoma and seminoma which suggests that they may more properly be referred to as atypical teratomas.

Topics: Acid Phosphatase; Adult; Alkaline Phosphatase; Anorexia Nervosa; Brain Neoplasms; Coma; Diabetes Insipidus; Dihydrolipoamide Dehydrogenase; Dysgerminoma; Electron Transport Complex IV; Esterases; Female; Humans; Hydrocortisone; Hypernatremia; Hypothalamus; Male; Osmolar Concentration; Oxidoreductases; Pinealoma; Sodium; Testicular Neoplasms; Thyroxine; Tuberculosis; Vasopressins

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Antigen-Antibody Reactions; Antilymphocyte Serum; BCG Vaccine; Cell Migration Inhibition; DNA; Guinea Pigs; Hypersensitivity, Delayed; In Vitro Techniques; Lymph Nodes; RNA; Spleen; Thymidine; Time Factors; Tritium; Tuberculin Test; Tuberculosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Antilymphocyte Serum; Autoradiography; BCG Vaccine; Cell Migration Inhibition; DNA; Guinea Pigs; Hypersensitivity; Hypersensitivity, Delayed; Lymph Nodes; Lymphocyte Activation; RNA; Spleen; Thymidine; Tritium; Tuberculin Test; Tuberculosis

Topics: Acid Phosphatase; Adult; Alkaline Phosphatase; Animals; Antibody Formation; Antigens; Cholelithiasis; Female; Glucuronidase; Hexosaminidases; Histocytochemistry; Humans; Lupus Erythematosus, Systemic; Lymph Nodes; Lymphocytes; Male; Peroxidases; Plasma Cells; Rabbits; Rats; Sarcoidosis; Stomach Neoplasms; Stomach Ulcer; Tuberculosis

Topics: Acid Phosphatase; Animals; Cell Fractionation; Lysosomes; Mice; Mycobacterium tuberculosis; Tuberculosis

Topics: Acid Phosphatase; Animals; Anti-Bacterial Agents; Cathepsins; Chromatography, Gel; Fatty Acids, Nonesterified; Lipids; Lung; Lysosomes; Male; Membranes; Mice; Mycobacterium; Mycobacterium bovis; Peptides; Phospholipids; Proteins; Tissue Extracts; Tuberculosis

Topics: Acid Phosphatase; Animals; Cell Count; Deoxyribonucleases; Esterases; Female; Glucuronidase; Lipase; Macrophages; Male; Muramidase; Pulmonary Alveoli; Rabbits; Radiation Injuries, Experimental; Ribonucleases; Tuberculosis; Tuberculosis, Pulmonary

Topics: Acid Phosphatase; Histamine; Humans; In Vitro Techniques; Neutrophils; Phagocytosis; Tuberculin; Tuberculosis

Topics: Acid Phosphatase; Animals; Antitubercular Agents; Bacterial Proteins; Centrifugation; Chromatography, Gel; Cytoplasmic Granules; Lung; Lysosomes; Mice; Mycobacterium; Mycobacterium bovis; Spleen; Tuberculosis

Topics: Acid Phosphatase; Animals; Cathepsins; Chromatography, Gel; Hydrogen-Ion Concentration; In Vitro Techniques; Lung; Lysosomes; Mice; Mycobacterium tuberculosis; Spleen; Tuberculosis

Topics: Acid Phosphatase; Animals; Ascitic Fluid; Guinea Pigs; Leukocytes; Male; Mycobacterium bovis; Tuberculosis; Virulence

Topics: Acid Phosphatase; Animals; BCG Vaccine; Centrifugation; Chromatography, DEAE-Cellulose; Chromatography, Gel; Hydrogen-Ion Concentration; Liver; Lung; Lysosomes; Mice; Models, Biological; Mycobacterium bovis; Mycobacterium tuberculosis; Proteins; Spleen; Staining and Labeling; Tuberculosis

Topics: Acid Phosphatase; Animals; Centrifugation; Chromatography; Chromatography, Gel; Hydrogen-Ion Concentration; Lung; Lysosomes; Mice; Mycobacterium bovis; Mycobacterium tuberculosis; Proteins; Spleen; Tissue Extracts; Tuberculosis

Topics: Acid Phosphatase; Animals; Glycoside Hydrolases; Guinea Pigs; Mice; NAD; Succinate Dehydrogenase; Tuberculosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Antitubercular Agents; Histocytochemistry; Lung; Rabbits; Tuberculosis

Topics: Acid Phosphatase; Animals; Arteriosclerosis; Bronchiectasis; Celiac Plexus; Collagen Diseases; Dogs; Emphysema; Ganglia, Autonomic; Histocytochemistry; Humans; Infections; Liver Cirrhosis; Neoplasms; Synapses; Tuberculosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Aminosalicylic Acids; Animals; Histocytochemistry; Isoniazid; Lung; Rabbits; Streptomycin; Tuberculosis

Topics: Acid Phosphatase; Diagnosis, Differential; Esterases; Granuloma; Humans; Lymph Nodes; Lysosomes; Prednisone; Sarcoidosis; Tuberculosis

Experiments are reported dealing with the increase of lysosomal acid hydrolases induced by BCG infection. Acid hydrolases were determined quantitatively in peritoneal MP, liver homogenate, and plasma of normal and BCG-infected mice. A significant increase of acid phosphatase, beta-glucuronidase, and cathepsin was found in MP and liver homogenate of BCG-infected mice. In plasma also a significant increase of acid phosphatase and beta-glucuronidase was noticed. The results of the determination of the enzymes in centrifugally separated subcellular fractions of liver homogenate indicated clearly that the acid hydrolases associated mainly with the "large granular" fraction, which consists of mitochondria, lysosomes, and microsomes and that infection with BCG caused significant increase of the enzymes specifically in this fraction. Differences in the pattern of location among centrifugally separated fraction of liver homogenate were observed between acid phosphatase and the other two acid hydrolases. MP cultured in vitro doubled their acid phosphatases content within 24 hours, whereas beta-glucuronidase rather decreased in the same cells.

Topics: Acid Phosphatase; Animals; Blood; Body Fluids; Cathepsins; Clinical Enzyme Tests; Cytoplasmic Granules; Electrons; Glucuronidase; Histocytochemistry; Hydrolases; Liver; Lysosomes; Mice; Microscopy; Microscopy, Electron; Mitochondria; Mononuclear Phagocyte System; Mycobacterium bovis; Peritoneum; Phagocytosis; Research; Tuberculosis

Experiments are reported dealing with the correlation between activities of lysosomal acid hydrolases and hyperreactivity to endotoxin induced by BCG infection. Acid hydrolases were determined quantitatively in peritoneal MP, liver homogenate, and plasma of normal and hyperreactive mice. Mice infected with BCG not only exhibited a hyperreactive state to lethal effect of endotoxin, but also responded to endotoxin by rapid increase of acid hydrolases, especially of beta-glucuronidase, in the plasma; whereas control mice responded to endotoxin by almost no change in plasma acid hydrolases. The extent of increase of beta-glucuronidase in plasma of hyperreactive mice was shown to correlate fairly well with the degree of hyperreactivity to the lethal effect of endotoxin. Desensitization of such animals with endotoxin was found to cause a decreased response of plasma beta-glucuronidase parallel with decreased mortality. A large amount of PPD exerted the similar effect to that of endotoxin in hyperreactive mice. Furthermore, the effect of PPD was decreased by desensitization of such animals with endotoxin, a fact which suggests contamination of PPD with endotoxin.

Topics: Acid Phosphatase; Animals; Blood; Clinical Enzyme Tests; Endotoxins; Escherichia coli; Glucuronidase; Hydrolases; Liver; Lysosomes; Mice; Mononuclear Phagocyte System; Mycobacterium bovis; Physiology; Research; Toxicology; Tuberculosis

Topics: Acid Phosphatase; Adolescent; Antitubercular Agents; Biochemical Phenomena; Biochemistry; Butyrates; Drug Therapy; Electron Transport Complex II; Enzymes; Glutamate Dehydrogenase; Glycerolphosphate Dehydrogenase; Humans; L-Lactate Dehydrogenase; Leukocyte Count; Leukocytes; Metabolism; Succinate Dehydrogenase; Tuberculosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Bronchiectasis; Diagnosis, Differential; Humans; Lung Abscess; Lung Neoplasms; Neoplasms; Serum; Tuberculosis; Tuberculosis, Pulmonary

Topics: Acid Phosphatase; Animals; Glucose-6-Phosphatase; Liver; Mice; Mononuclear Phagocyte System; Nitrophenols; Physiology; Research; Spleen; Tuberculosis

Topics: Acid Phosphatase; Adolescent; Alkaline Phosphatase; Arthritis; Arthritis, Infectious; Arthritis, Rheumatoid; Chemistry Techniques, Analytical; Diagnosis; Geriatrics; Gout; Humans; Knee Injuries; Osteoarthritis; Phosphoric Monoester Hydrolases; Synovial Fluid; Synovitis; Tuberculosis; Tuberculosis, Osteoarticular

Topics: Acid Phosphatase; Alkaline Phosphatase; Exudates and Transudates; Glucosidases; Leukocytes; Muramidase; Peritoneal Cavity; Tuberculosis

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Arthritis; Aspartate Aminotransferases; D-Alanine Transaminase; Fructose-Bisphosphate Aldolase; Humans; Hydrarthrosis; Joint Diseases; L-Lactate Dehydrogenase; Synovial Fluid; Tuberculosis; Tuberculosis, Osteoarticular

Topics: Acid Phosphatase; Adenoma; Alkaline Phosphatase; Ameloblastoma; Arthritis; Bone Cysts; Bone Neoplasms; Chondrosarcoma; Fibroma; Fibrous Dysplasia of Bone; Geriatrics; Giant Cell Tumors; Humans; Neoplasm Metastasis; Osteitis Fibrosa Cystica; Osteoma; Osteosarcoma; Prognosis; Radiography; Sarcoma, Ewing; Tuberculosis; Tuberculosis, Osteoarticular

Topics: Acid Phosphatase; Phosphoric Monoester Hydrolases; Research; Silicosis; Tuberculosis; Tuberculosis, Pulmonary