Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

A total of 25 apparently healthy adults (13 men and 12 women), 29.5 years (SD = 3.6 years) of age, served as subjects in a 24-h study conducted in Barcelona, Spain, in the spring of 1990. The group had a homogeneous pattern of meals, activity, and behavior. Six blood samples were collected at 4-h intervals over a single 24-h period beginning at 10:00 h. The oral temperature was measured at 2-h intervals to facilitate an independent biological time reference for the local population being studied. The serum concentration of 12 enzymes of clinical interest were measured in each sample: creatine kinase, creatine kinase 2, alanine aminotransferase, aspartate aminotransferase, gamma-glutamyltransferase, alkaline phosphatase, cholinesterase, lactate dehydrogenase, lactate dehydrogenase 1, 5'-nucleotidase, pancreatic alpha-amylase, and triacylglycerol lipase. We supposed that all experimental data obtained for a quantity came from a single "hypothetical subject" that represented the central tendency of the population and then these data were analyzed for circadian rhythm by single cosinor. A statistically significant circadian rhythm was detected in all quantities studied (p < or = 0.05) except for serum concentrations of pancreatic alpha-amylase and triacylglycerol lipase. The maximum daily rhythmic variation was approximately 10% (interval, 6-14%) for all quantities studied except pancreatic alpha-amylase (2.6%). This rhythmic variation is greater than the analytical variation except for 5'-nucleotidase and pancreatic alpha-amylase. The acrophases for the quantities studied (except that of triacylglycerol lipase) coincide with times near those of the oral temperature acrophase (18:01 local time). The results of this study will doubtless contribute to further documentation of the structure of the human circadian timing system and to establishment of time-qualified reference intervals for a defined group of subjects.
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PMID:Circadian rhythms of serum concentrations of 12 enzymes of clinical interest. 810 Apr 88

In prsA (protein secretion) mutants of Bacillus subtilis, decreased levels of exoproteins, including alpha-amylase and subtilisins, are found extracellularly. The effect of prsA on subtilisin secretion is elaborated here. Extracytoplasmic folding and secretion of active subtilisin is assisted by the N-terminal pro-sequence of its precursor. In this paper we present evidence that the product of the prsA gene is additionally required for these processes in vivo. We examined inducible expression of different subtilisin-alkaline phosphatase fusion genes in the prsA3 mutant. We found massive degradation of the fusion proteins, and a lack of enzymatic activity in the protein secreted. We suggest that PrsA is a novel chaperone with a predicted extracytoplasmic location, and is important in vivo for the proper conformation of various exoproteins, including those with pro-sequence (like subtilisin) and those without (like alpha-amylase).
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PMID:Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-sequences. 810 73

Total protein and activities of: alpha-amylase, alkaline phosphatase, alanine aminotransferase and aspartate aminotransferase in haemolymph of the freshwater snail Lymnaea stagnalis, naturally infected with digenetic larvae were investigated. There were no any changes in these parameters in the snails infected with Cercaria tenuispina that occupies mainly hematocele sinuses. Significant increase of activities of all examined enzymes in haemolymph of the snails infected with larvae belonging to the Furcocercariae group was ascertained. These changes were proportional to the degree of injury of the digestive gland, examined with the use of the thymol turbidity test. Total protein level was significantly higher only in haemolymph of snails with higher values of this test.
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PMID:[Level of total protein and activities of selected enzymes in hemolymph of Lymnaea stagnalis (L.) (Gastropoda: Pulmonata) naturally infected with digenetic fluke larvae]. 823 8

The effect of hemolysis on several assays performed with the Hitachi 717 was quantified by relating the amount of error to the concentration of hemoglobin. Hemolysis interference was judged clinically significant when analyte concentration varied by > 10% from the initial value. Hemolysis interference was significant for alkaline phosphatase, aspartate aminotransferase, alpha-amylase, bilirubin, creatine kinase, gamma-glutamyltransferase, lactate dehydrogenase, lactate dehydrogenase-1, potassium, and theophylline assays. Error (expressed in absolute terms) was linearly dependent on hemoglobin concentration and independent of the initial analyte concentration in each case, except for bilirubin and theophylline, where multiple regression analysis was required to quantify the effect. Relative error was dependent on the initial analyte concentration in all cases. Correction formulas were calculated from linear regression of absolute error vs hemoglobin concentration. Clinical application of correction formulas and mechanisms of hemolysis interference for each assay are discussed.
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PMID:Characterization and mathematical correction of hemolysis interference in selected Hitachi 717 assays. 837 45

Commercial serum preparations are integral components of both internal and external quality control programs for enzyme activity measurements. However, properties of these materials may differ significantly from those of clinical specimens. Differences from clinical specimens may include the following: species origin of the enzyme; isoenzyme form(s); integrity of the molecular species; matrix of the solution; processes such as lyophilization; and addition of preservatives. There are also significant differences among methods measuring the activity of a single enzyme including a diversity of compounds that may serve as substrate(s); variable cofactor or metal supplementation; and differences in the substrate concentration(s), buffer substances, pH, and temperature. The measured response to each of these variations in assay technique may differ among these types of specimens. To be acceptable, quality control materials must have properties similar to those of clinical specimens. Thus, the concept of commutability that we originated and first applied to enzyme activity measurements remains useful, and its further application to the problem of "matrix effects" is reviewed here. Multivariate display techniques are applied to the specific examples of aspartate aminotransferase, alpha-amylase, and alkaline phosphatase to judge the commutability of quality control materials for these enzymes.
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PMID:Accurate enzyme activity measurements. Two decades of development in the commutability of enzyme quality control materials. 846 97

Sixty two samples of amniotic fluid were submitted to biochemical investigation including 31 samples from women with pregnancy complicated by hypertension (studied group with blood pressure -65 +/- 15/95 +/- 5 mm Hg) and 31 samples deriving from healthy pregnant women (control group with mean blood pressure 118 +/- 10/74 +/- +/- 9 mm Hg). The following parameters of amniotic fluid were measured: 1) aminotransferases: alanine AlAT and aspartate AspAT, 2) alkaline phosphatase (APt) and its thermostable isoenzyme (APh), 3) ceruloplasmin (Crlp), 4) alpha-amylase (alpha-Amy). The study showed pregnancy complicated by hypertension is related to fetal salivary gland's immaturity presenting decreased activity of alpha amylase in amniotic fluid. Amniotic fluids deriving from women with pregnancy complicated by hypertension showed normal activities of AlAT, AspAT, APt, APh and Crlp.
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PMID:[Evaluation of fetal condition in pregnancy complicated by hypertension--biochemical assessment of amniotic fluid. II. Enzymes]. 928 52

Dibutyltin dichloride (DBTC; 6 mg/kg body weight, i.v.) induced acute interstitial pancreatitis in rats. The course of the pancreatitis was examined within 28 days by light and electron microscopy as well as by pathobiochemistry (amylase, lipase, alkaline phosphatase, and bilirubin in serum; tin concentration in biliopancreatic juice, tissue, and concretions). The pathogenesis of the DBTC-induced pancreatitis in rats was studied by different experimental designs (in intact animals, after bile duct ligation, after surgical bypass of the bile duct). DBTC caused toxic necrosis of the biliopancreatic duct epithelium, which is then shed into the duct and forms obstructing plugs in the distal common bile duct. Interstitial pancreatitis occurred during the first 4 days, accompanied by significantly increased activities of serum alpha-amylase and lipase. After 7 days extensive infiltration of the pancreatic interstitium with mononuclear cells was observed. Twenty-eight days after administration of DBTC one-third of the rats showed periductal and interstitial fibrosis as well as an active inflammatory process in the pancreas. The findings suggest a twofold pathogenesis of the DBTC-induced pancreatitis: first, the cytotoxic effects on the biliopancreatic duct epithelium lead to epithelial necrosis with obstruction of the duct, subsequent cholestasis, and interstitial pancreatitis; and second, the hematogenic DBTC effects cause direct injury of pancreatic cells (mitochondrial damage, autophagy, cell necrosis) followed by interstitial edema and inflammation. Both processes lead to this special type of DBTC-induced acute pancreatitis with a tendency to a chronic course, when the obstruction of the duct and cholestasis persist.
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PMID:Acute interstitial pancreatitis in rats induced by dibutyltin dichloride (DBTC): pathogenesis and natural course of lesions. 936 Oct 94

Enzymatic ejaculates activity was studied in 15 fertile and 65 subfertile samples of human sperm. The activity of alkaline phosphatase (EC 3.1.3.1), alpha-amylase (EC 3.2.1.1), gamma-glutamyl transferase (EC 2.3.2.2), creatine kinase (EC 2.7.3.2), total lactate dehydrogenase (EC 1.1.1.27) and lactate dehydrogenase-1 was compared to spermogram findings according to 14 morphological and physicochemical criteria of fertility. The enzyme activity depends on functioning of the testes, seminal vesiculae, prostate, bulbourethral glands and is involved in formation of fertility. The findings allowed elucidation of the role of synthesis and some function of spermoplasma enzymes. Practical applications of the above data are discussed in the treatment of male infertility and to raise fertilizing power of the sperm in artificial insemination.
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PMID:[The enzymatic activity of the seminal plasma in ejaculates of different fertilities]. 941 13

The kinetic method revealed that by the rate of adsorption on apatite, serum alkaline phosphatase (AlP) is homologous and salivary AlP consists of two fractions: "slow" with the constant of adsorption rate approximating that of serum AlP and "fast" with 5-6 times greater constant. A mechanism of phosphatase immobilization on apatite by two-stage sequential reaction is proposed. The constants of rates of both stages for the serum phosphatase and fast salivary fraction are determined. Difference of the products of both stages by the Michaelis constant (KM) is demonstrated for the fast fraction. The KM of the second-stage immobilization product is close to that of AlP immobilized on dental enamel, which confirms the hypothesis about their identity. In contrast to AlP, both serum and salivary alpha-amylase react with apatite at the same rate and, probably, by the same mechanism as the bulk of salivary and serum protein.
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PMID:[The possible mechanisms of alkaline phosphatase and alpha-amylase immobilization in dental enamel]. 947 22

Knottins are a group of small, disulphide-bonded proteins that bind with high specificity to their target molecules. These proteins appear to use different faces of the protein for their interactions with different targets. Here, we attempted to create knottins with novel binding activities based on the cellulose-binding domain of the fungal enzyme cellobiohydrolase I. Variation was introduced to the face of the protein that binds cellulose. Seven residues, which are located in two regions of the polypeptide chain and form a patch of about 400 A2 on the protein surface, were simultaneously varied by random mutation of the gene. The repertoire was cloned for display on filamentous bacteriophage (5.5 x 10(8) clones), and selected for binding to cellulose or to one of three enzymes (alpha-amylase, alkaline phosphatase and beta-glucuronidase). We thereby isolated variant knottins against cellulose (differing in sequence from the parent knottin) and also against alkaline phosphatase. The binding to (glycosylated) alkaline phosphatase was highly specific with an affinity of about 10 microM, required the presence of disulphide bonds and was mediated through protein (rather than carbohydrate) contacts. Knottin scaffolds therefore appear to be a promising architecture for the creation of small folded proteins with binding activities, with the potential for improvement of binding affinities by mutation, or of using other faces of the protein to provide greater structural diversity in the primary repertoire.
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PMID:Small binding proteins selected from a combinatorial repertoire of knottins displayed on phage. 951 63


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