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)

The study of isoenzymes is often of great interest in clinical biology however, as far as alkaline phosphatase is concerned, no simple method is available to evaluate the forms of bony, intestinal, hepatic or placental origin. In most cases, it is necessary to combine several technic: electrophoresis, denaturation by heat, urea or phenyl alanine. This already complex analytical problem is rendered still more difficult by the choice of reference isoenzyme to be used calibration of the technic. The interest of this determination, especially in the field of oncology and pediatrics, should however encourage the biologist to pursue this route.
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PMID:[Alkaline phosphatase isoenzymes in human serum]. 35 97

Liver injury was investigated in the course of salmonellosis evoked by Salmonella agona in experimental infection of rabbits. Histological and biochemical examination (proteinogram, the level of bilirubin, fibrinogen, cholesterol and its esters in blood, activity of asparine and alanine aminotransferases and alkaline phosphatase and guanase in blood) were carried out in 70 animals. Liver injury showing degeneration, steatosis and necrosis was found in the course of salmonellosis. Hepatitis gigantocellularis was sporadically observed. Biochemical parameters were not in correlation with the observed histological changes.
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PMID:Injury of liver in experimental salmonellosis of rabbits infected by salmonella agona. 42 97

The overall transport of bile salts across the hepatocyte is characterized as a carrier-mediated process whose rate-limiting step is biliary secretion. Specific bile salt binding proteins have been identified in liver surface membrane fractions and were postulated to represent the initial interaction in bile salt translocation across both the sinusoidal and canalicular membranes. To test this hypothesis, cycloheximide was administered to rats to inhibit hepatic protein synthesis. 16 h after cycloheximide administration [14C]leucine incorporation into hepatic protein was inhibited by 93% at 1 h and 47% at 12 h. However, values of liver function tests were not increased, although serum albumin, serum alanine amino-transferase, and alkaline phosphatase were significantly decreased. Light and electron microscopy did not demonstrate necrosis or fat accumulation. The latter demonstrated minimal disorganization of rough endoplasmic reticulum and occasional lamellar whorls. 16 h after cycloheximide administration bile salt independent bile flow, basal bile salt excretion, and basal bile flow were unaltered, but the maximum bile salt transport capacity was reduced to 62% of control and 24 h later to 38%. Decreased bile salt transport was reversible, for it returned to control values after 48 h, when hepatic protein synthesis was also normal. Maximum bromosulfophthalein (BSP) transport, on the other hand, was reduced after 16 h to only 85% of control. Both bile salt and BPS maximum transport capacities decreased with time during inhibition of protein synthesis, apparently following first order kinetics. It was estimated that their half-lives are 20 h for bile salt transport and 55 h for BSP transport. These different turnover rates suggest that cycloheximide does not decrease active transport through generalized hepatic dysfunction or alteration of high energy sources possibly required for transport. The maximum number of [14C]cholic acid binding sites in liver surface membrane fractions was determined by an ultrafiltration assay. They were reduced to 68% of control after 16 h of cycloheximide and to 25% after 24 h. This reduction in the number of binding sites is apparently selective, for the activities of the liver surface membrane enzymes (Na+-K+)ATPase, Mg++-ATPase, and 5'-nucleotidase were not significantly changed. The associated alterations in bile salt transport and the maximum number of binding sites after cycloheximide administration suggests that these receptors may be the bile salt carriers.
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PMID:Regulation of hepatic transport of bile salt. Effect of protein synthesis inhibition on excretion of bile salts and their binding to liver surface membrane fractions. 43 30

A pattern of results is reported which was found to be common among patients who had intrahepatic cholestasis (IHC) which was rarely found in patients with other hepatic conditions. The pattern was recognized from over 1000 cases suspected of hepatobiliary disease. 29 were diagnosed with IHC, and excluding 4, 25 revealed the following etiological pattern: chlorpromazine (12 patients); pregnancy and oral contraceptive use (8); and other (5). As opposed to patients with acute and chronic hepatic disease, IHC sufferers had relatively normal values for immunoglobulins and antibody titers. A disproportionate elevation of serum bilirubin vis-a-vis serum enzymatic activities separated potential IHC cases into intra- and extrahepatic cholestasis. The following factorial evaluations were useful in distinguishing hepatic disease states: 1) when the sum of the activities of serum alkaline phosphatase, 5'-nucleotidase, aspartate and alanine amiotransferases, and isocitrate dehydrogenase was divided by the serum bilirubin concentration, there was good resolution of the distinction between patients with IHC and those with primary biliary cirrhosis, early and late viral hepatitis, cholelithiasis, and pancreatic and bile duct cancers. 2) Resolution was also achieved when the numerator included alkaline phosphatase, 5'-nucleotidase, and aspartate aminotransferase, but not when alkaline phosphatase alone, or alkaline phosphatase combined with 5'-nucleotidase, was used. The essential lesion in IHC is an excretory defect.
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PMID:Biochemical features of intrahepatic cholestasis. 45 73

Treatment of rats with cefazolin in vivo significantly suppressed activity of alanine and aspartate aminotransferases in serum and in the liver, brain, kidney, and heart. Simultaneous administration of pyridoxal further reduced enzyme activity except in the liver, where there was no change. Pyridoxal 5'-phosphate partly reversed the decreased enzyme activity in the serum, liver, and kidney, but did not return it to the amount observed in the control animals; enzyme activity remained suppressed in the brain and heart. The effect of cefazolin was dose related, but there was no sex-related difference. In contrast to its action on am-notransferase activity, cefazolin elicited no effect on alkaline phosphatase (pyridoxal-5'-phosphate hydrolase) in serum or on pyruvate carboxylase in the liver, heart, and kidney. Cefazolin exposed to the hepatic microsomal mixed-function oxidase system in vitro was partly converted into metabolites that inhibited serum alanine aminotransferase activity in vitro. The latter inhibition was reversed by the addition of pyridoxal 5'-phosphate.
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PMID:Decreased aminotransferase activity of serum and various tissues in the rat after cefazolin treatment. 45 47

Semen samples were collected at weekly intervals for six weeks from eight sexually mature beagles previously shown to produce normal ejaculates. Seminal plasma and sperm fractions were separated by centrifugation and the sodium, potassium, alanine and aspartate aminotransferases, acid and alkaline phosphatase concentrations in the two fractions determined. Regression analysis of the mean weekly values obtained from physical and biochemical examination of the ejaculates showed that sodium ion concentration was highest in seminal plasma. The highest levels of aminotransferases were found in sperm fractions. Those enzymes may be indices of abnormal or damaged spermatozoa. Acid and alkaline phosphatase activity was 100 times greater in seminal plasma than in sperm fractions. Phosphatase concentrations are likely to be dependent on prostate activity. Measurement of acid phosphatase in canine semen therefore may be a useful index of prostate function. The motility of the semen samples was independent of the potassium concentration in seminal plasma. However, there was some evidence of a correlation between sperm motility and the enzyme and sodium content of seminal plasma.
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PMID:Biochemical observations on beagle dog semen. 47 66

Brush border sucrase and alkaline phosphatase activities are considerably enhanced in the intestine of ascorbic acid deficient guinea-pigs. Similar increase in the uptake of D-glucose and L-alanine also occurs in chronic vitamin C deficiency. However the permeability of D-glucose and L-alanine in the intestine of animals fed with large doses of vitamin C is severely depressed, with a reduction in the levels of sucrase and alkaline phosphatase activities.
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PMID:Effect of chronic hypo and hypervitaminosis C on the brush border enzymes and the intestinal uptake of glucose and alanine. 47 73

We describe a mechanized method for centrifugal analyzer determination of sorbitol dehydrogenase in serum, based on conversion of D-fructose to sorbitol with simultaneous oxidation of NADH, in triethanolamine buffer at pH 7.4 and 30 degrees C. The standard curve for this assay is linear to 200 U of activity per liter of serum. The mean within-run precision (CV) of the assay is 0.8%. Results correlate well with those by a spectrophotometric method. In sera from 20 apparently healthy adult humans, sorbitol dehydrogenase activity averaged 1.7 (SD +/- 0.8; range, 1-3) U/L. The mean activity (U/L) for a group of 30 rats was 4.4 (SD, +/- 0.2; range, 3-6); for 20 dogs, 5.8 (SD, +/- 0.7; range 3-9); and for 30 mice, 26.8 (SD +/- 2.1; range, 22-34). To determine the utility of measuring this enzyme in the serum of rats for assessment of hepatotoxicity in drug-safety studies, we compared sorbitol dehydrogenase activity with that of alkaline phosphatase, aspartate aminotransferase, and alanine aminotranferase in the sera of rats treated with thioacetamide or in which the common bile duct has been ligated.
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PMID:Kinetic determination of serum sorbitol dehydrogenase activity with a centrifugal analyzer. 50

Activities of lactate dehydrogenase /LDH/, glucose-6-phosphate dehydrogenase /G6PD/, transaminases, alkaline phosphatase as well as content of lactic acid were studied in enterolysed parts of gastric mucose and in normal mucose. The LDH activity and content of lactic acid were decreased in the enterolysed mucose. As compared with normal mucose the activity of G6PD was increased 3-fold, activities of alkaline phosphatase and of glutamine-alanine transaminases were increased 1.5-2-fold in the mucose regions with metaplasia. In vitro glycocholic acid and products of duodenal secretion inhibited distinctly G6PD and LDH within 10 min of incubation; maximal activity of G6PD was observed within 20 min, after addition of cholic acid the enzyme was completely inactivated within 30 min. Under these conditions the activity of alkaline phosphatase was decreased within 10 min and returned up to the initial level within the subsequent periods.
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PMID:[Enzymatic activity in the enterolysed portions of the human gastric mucosa in peptic ulcer and the effect of bile]. 51 30

The determination of the activity of alkaline phosphatase (AP)--orthophosphate-monoesterphosphohydrolase, EC.3.1.3.1.--and alanine-aminopeptidase (ANA)--alpha-aminoacyl-peptide hydrolase (microsomal), EC.3.4.11.2--in the serum of non-gravid and gravid women has shown that in non-gravid women normal ANA values range from 17.0 to 32.0 I. U. and normal AP values from 14.4 to 26.0 I. U., the ANA/AP quotient amounting to 1.28 (S = +/- 0.301 I. U., KV = 23.5%, n = 29). The determination of the activity of the above quoted enzymes has shown that in the course of pregnancy the values of both enzymes increased by the exponential curve which allowed the calculation of the ANA/AP quotient for each month of pregnancy. The ANA/AP quotient determined in this way is proposed to serve as a diagnostic parameter in the routine control of pregnant women.
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PMID:[Relationship between the activity of alanine aminopeptidase and alkaline phosphatase in the blood of pregnant women]. 61 66


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