Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Most of the enzymes used in routine biochemical tests have been detected in circulating enzyme-linked immunoglobulin (Ig) complexes (E-Ig). The complexes often cause unexplained hyperenzymemia and give anomalous patterns on isozyme electrophoresis. However, E-Ig does not appear to be associated with any pathological conditions. The present study was undertaken to determine the clinical characteristics of patients with E-Ig. More than 42,000 patients selected at random and 10,000 blood donors were screened for lactate dehydrogenase (LDH)-linked Ig complexes (LDH-Ig), amylase (Amy)-linked Ig complexes (Amy-Ig), alkaline phosphatase (AP)-linked Ig complexes (AP-Ig) and creatine kinase (CK)-linked Ig complexes (CK-Ig). LDH-Ig and Amy-Ig were screened by electrophoresis for routine isozyme analysis and identified by precipitin reactions. AP-Ig and CK-Ig were screened and identified by counter immunoelectrophoresis. The incidence of all E-Ig ranged from 0.18% to 0.61% in patients and from 0.03% to 0.23% in blood donors. The incidence curves of E-Ig were age-related, generally increasing with age. The curves of E-IgG's for different enzymes resembled each other in shape but those of E-IgA's did not. A positive correlation between E-IgG and autoimmune diseases was present. Consequently, it is concluded that both autoimmune diseases and age are the common clinical factors involved in E-IgG. No specific diseases were found for cases with E-IgA. However, it is suggested that some CK-IgA, but not all, is caused by elevated serum CK activity.
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PMID:Enzyme-linked immunoglobulins and their clinical significance. 280 13

The local and systemic pathological changes induced by an i.m. injection of 100 micrograms of Bothrops asper venom in mice were studied histologically and by following the changes in serum levels of enzymes, proteins, ATP and lactate, as well as alterations in hematocrit and clotting time. B. asper venom induced a rapid and marked increase in serum levels of creatine kinase, aspartate aminotransferase and lactate dehydrogenase, but not alanine aminotransferase or alkaline phosphatase. A local myonecrosis and hemorrhage was observed, with the lungs collapsing by 24 hr and the kidneys showing glomerular congestion and vacuolar degeneration of tubular cells. Only minor histopathological changes were observed in cardiac muscle and liver. Both ATP and lactate blood levels decreased after venom injection, whereas there were no changes in serum protein concentration. Blood incoagulability was observed 1 and 3 hr after envenomation. Antivenom neutralized venom-induced increases in serum enzyme levels following preincubation with venom, indicating that antivenom contains antibodies against tissue-damaging toxins. However, when antivenom was administered i.v. at different time intervals after venom injection, neutralization was only partial, with the exception of defibrinating activity, which was totally neutralized even after a delay of 1 hr in administering antivenom.
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PMID:Histopathological and biochemical alterations induced by intramuscular injection of Bothrops asper (terciopelo) venom in mice. 281 6

This study was prompted by the paradox of strong presence of mitochondria in an anaerobic protozoan, recently reclassified from the yeasts. Stemming from publication in 1911 to 1912, Blastocystis hominis has been generally accepted as a harmless intestinal yeast of humans, with short standardized textbook (parasitology) descriptions, even to the present day. Reports since 1967 have changed the classification of B. hominis from yeast to protozoan (Sarcodina), and this has been followed by interest in B. hominis-caused disease, resulting in documentation of disease in humans and other primates. In this study of B. hominis, the basic ultrastructure of the mitochondria was shown by thin-section electron microscopy to be identical to that of an archetypical mitochondrion. There were hundreds of them in large B. hominis cells (100 to 200 microns in diameter). Mitochondria were confined to a peripheral ring of cytoplasm bounded by the outer cell membrane (there is no cell wall) and the membrane of the large, spherical, organelle-free central body that constitutes 75% of the cell's volume. Mitochondria tended to surround the cell's usual two to four nuclei. Rhodamine 123 stained the mitochondria selectively, visualized by fluorescence microscopy. The cell was devoid of cytochromes. Addition of 0.1% cytochrome c to the growth medium increased utilization of glucose by 34% and that of lactate by 17%. Furthermore, it markedly increased the number of mitochondrion-filled cells. At higher concentrations, cytochrome c inhibited the growth of the cells. Despite the presence of large numbers of mitochondria, activities of the mitochondrial enzymes pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex, isocitrate dehydrogenase, glutamate dehydrogenase, and cytochrome c oxidase were absent. Thus, the function of the mitochondria in B. hominis remains unknown. Considerable activities of aspartate aminotransferase and alanine aminotransferase were found. Aldolase activity was prominent. Pyruvate decarboxylase was present. Diaphorase and lactate dehydrogenase were detectable but in suspect quantities. Other missing enzymes were gamma glutamyl transpeptidase, alkaline phosphatase (a lysosomal marker), and creatine kinase isoenzymes.
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PMID:Biochemical and ultrastructural study of Blastocystis hominis. 283 9

The activities of 4 enzymes, i.e. alkaline phosphatase, gamma-glutamyl transferase, lactate dehydrogenase and creatine kinase were studied in bronchial aspirates and serums from two groups of subjects, the first one was composed of 14 subjects without active bronchopulmonary pathology and the other of 20 patients with lung cancer. The results showed a statistically significant decrease of the activities of alkaline phosphatase and beta-glutamyl transferase in bronchial aspirate from patients with bronchogenic malignant tumors in relation to normal subjects. This finding could be explained by the 'fetalism' principle, which states that the quantitative pattern of enzymes of immature human tissues resembles those of neoplastic tissues.
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PMID:Alkaline phosphatase, gamma-glutamyl transferase, lactate dehydrogenase and creatine kinase in bronchial aspirate from neoplastic and normal pulmonary tissue. 286 Oct 86

The stability and storage characteristics were studied of 11 bovine enzymes of potential clinical significance, namely, aldolase, alkaline phosphatase, alanine aminotransferase, aspartate aminotransferase, acetylcholinesterase, creatine kinase, gamma glutamyltransferase, glutathione peroxidase (GSH-Px), alpha-hydroxybutyrate dehydrogenase, lactate dehydrogenase and superoxide dismutase (SOD). Enzyme activities in fresh serum were compared with those in plasma containing various anticoagulants including lithium heparin, EDTA and oxalate/fluoride. The same preservatives were assessed for their effects on the whole blood activities of GSH-Px and SOD. Stabilities of enzymes in plasma and serum stored at room (+20 degrees C), refrigerator (4 degrees C) or deep freeze (-20 degrees C) temperatures were also compared. In addition, SOD and GSH-Px activities in samples stored, at the same temperatures, as whole blood or aqueous lysates were monitored.
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PMID:Stability and storage characteristics of enzymes in cattle blood. 286 28

The stability and storage characteristics were studied of 11 ovine enzymes of potential clinical significance, namely, aldolase, alkaline phosphatase, alanine aminotransferase, aspartate aminotransferase, acetylcholinesterase, creatine kinase, gamma glutamyltransferase, glutathione peroxidase (GSH-Px), alpha-hydroxybutyrate dehydrogenase, lactate dehydrogenase and superoxide dismutase (SOD). Enzyme activities in fresh serum were compared with those in plasma containing various anticoagulants including lithium heparin, EDTA and oxalate/fluoride. The same preservatives were assessed for their effects on the whole blood activities of GSH-Px and SOD. Stabilities of enzymes in plasma and serum stored at room (+20 degrees C), refrigerator (4 degrees C) or deep freeze (-20 degrees C) temperatures were also compared. In addition, SOD and GSH-Px activities in samples stored, at the same temperatures, as whole blood or aqueous lysates were monitored. The results are discussed with particular reference to the differences between sheep and cattle.
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PMID:Stability and storage characteristics of enzymes in sheep blood. 286 29

The plasma electrolytes, Na+, K+, Ca2+, Cl- and osmolarities had high values in capture-stressed big gamefish. Blood metabolites measured after stress showed glucose and lactate elevations. The activity of the plasma enzymes alkaline phosphatase, alanine aminotransferase, aspartate aminotransferase, creatine kinase and lactate dehydrogenase suggested tissue disruptions following severe capture stress. Haematocrit values and methaemoglobin were high in capture-stressed gamefish. The plasma chemistry of resting and capture-stressed snapper (Chrysophrys auratus) was studied for comparison. Specific differences in plasma biochemistry appeared to be the result of different strategies of fish behaviour during capture.
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PMID:Physiological stress responses in big gamefish after capture: observations on plasma chemistry and blood factors. 287 36

We evaluated the performance of the Kodak DTSC Module for determination of alanine aminotransferase (ALT; EC 2.6.1.2), aspartate aminotransferase (2.5.1.2), alkaline phosphatase (3.1.3.1), creatine kinase (2.7.3.2), gamma-glutamyltransferase (2.3.2.2), and lactate dehydrogenase (1.1.1.27). The DTSC is a "special chemistry" accessory for the DT60 analyzer; the same multilayer film technology as that of the Ektachem 700 is used. The overall precision, assessed over a three-month period with two serum-based quality control materials, ranged from 2.2 to 8.0%. DTSC results for patients' specimens correlated well with those by the Technicon RA-1000 analyzer. The performance of the analyzer in linearity and interference studies was satisfactory for clinical use. The DTSC is simple to operate and has no technique-dependent step; it should be useful for the physician's office laboratory.
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PMID:Measurement of six enzymes with the Kodak DTSC Module, a physician's office analyzer. 288 44

(1) Sexually immature and mature rats were fed a nutritionally-complete liquid diet or isovolumetric quantities of the same diet in which 36% of the calories as glucose were substituted by isocaloric ethanol. (2) After 6 weeks ethanol feeding, significant reductions in body weight (approx. 15%) occurred in both groups of rats. In immature rats there were significant reductions (7-21%) in bone, gastrocnemius, liver, and skin weights. The total skeletal muscle mass was reduced by 20%. Lung and kidney weights were not significantly altered. In mature rats smaller decreases in organ weights were found, which were only significant for skeletal muscle and skin. The gastrocnemius protein content was significantly reduced in immature but not in mature rats. Plasma protein concentrations were unaltered in both groups. (3) Plasma aspartate aminotransaminase, gamma glutamyl transferase and creatine kinase activities in immature and mature rats were not significantly altered by ethanol feeding, but there were increases in plasma alkaline phosphatase activities in immature, but not in mature, rats. Plasma glucose was slightly raised by ethanol feeding in immature but not mature rats. Plasma triglycerides and insulin were unaltered in both groups of rats. (4) Protein synthesis was measured with a flooding dose of L[4(3)H]-phenylalanine. Rates of protein breakdown were calculated from the difference between synthesis and growth. Fractional and absolute rates of skeletal muscle protein synthesis were reduced by 13-30% by ethanol treatment, in immature and mature rats. Fractional rates of protein breakdown were also reduced by ethanol, by 13 and 19% in immature and mature rats, respectively.
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PMID:The effect of chronic ethanol feeding on body and plasma composition and rates of skeletal muscle protein turnover in the rat. 290 20

Acute renal failure was diagnosed by clinical, necropsy and histological criteria in 39 flocks (20 low ground, 13 hill and six marginal upland) in areas served by six veterinary investigation centres. Forty-eight lambs of 12 different breeds or crosses were investigated. The mean age of affected lambs was 38 days (range seven to 84 days); 21 lambs (44 per cent) were aged seven to 28 days, while only eight (17 per cent) were older than two months. Mortality in clinically affected lambs was almost 100 per cent, with no response to various treatments. Histological examination showed that 40 lambs (83 per cent) had nephrosis, while the rest had toxic tubular necrosis, interstitial nephritis or tubular damage associated with oxalate crystal deposits. Only about half of the lambs had any evidence of enteric infections or enteropathy. Acutely ill lambs had azotaemia, haemoconcentration and proteinuria; some lambs had glycosuria or haematuria. Samples of plasma from 22 lambs with nephrosis were compared with similar samples from 82 incontact but asymptomatic lambs. The clinically affected group had significantly elevated plasma urea, creatinine, total protein, globulin, phosphorus and chloride concentrations and significantly reduced plasma calcium concentrations compared with healthy lambs. Affected lambs had a significant reduction also in the calcium:phosphorus ratio. No significant differences between groups was found in plasma concentrations of albumin, glucose, lactate, glycerol, creatine kinase, alkaline phosphatase, sodium, potassium or magnesium.
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PMID:Acute nephropathy in young lambs. 291 11


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