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

The most frequently estimated enzyme-activities in the serum of children are discussed; these are the serum transaminases GOT and GPT, gamma-GT, alkaline phosphatase, lactate and hydroxy-butyrate dehydrogenase, as well as the creatinkinase and the alpha-amylase. The limited significance of these results for the diagnosis or prognosis is shown. A pattern of several enzyme-activities allows for a better judgement of a situation than the measurement of only one enzyme. Nowadays easier isoenzyme determinations allow for an organ-specific diagnosis. The inherited rise of alkaline phosphatase activity in the absence of disease is known, equally the idiopathic rise of creatinkinase and alpha-amylase. All results of enzyme-activity measurements should be judged in the context if the clinical situation.
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PMID:[Clinical significance of the measurement of serum enzyme activity in children]. 286 32

The average biological intra-individual CV in 20 patients with chronic liver diseases (CLD), estimated for 14 analytes during a stationary phase, significantly exceeded that for a normal group in the cases of Na+, K+, Cl-, total protein, albumin, cholinesterase, hemoglobin, and alpha-amylase; it did not differ significantly from the normal group for cholesterol, alkaline phosphatase, aspartate aminotransferase, and alanine aminopeptidase; and it was significantly lower than in the normal group for alanine aminotransferase and gamma-glutamyltransferase. There were no significant sex-related differences in mean intra-individual variation in CLD patients. Individual values were gaussian-distributed for all analytes, including enzymes. The estimated biological component of intra-individual variation and the analytical variation as determined for each laboratory can be used to derive decision-making criteria in monitoring CLD.
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PMID:Intra-individual variation of analytes in serum from patients with chronic liver diseases. 288 11

This study identifies the in vitro differences (markers) between virulent and attenuated transmissible gastroenteritis (TGE) viruses. Exposure of virulent Miller strain and attenuated Purdue strain TGE viruses to a spectrum of acidities indicated that the Miller strain was more stable at pH 2. Acidities at or above pH 3 did not reduce viral infectivity of either strain. When virulent and attenuated viruses were exposed to gastric fluids of either fed or fasted swine, there was a similar degree of sensitivity. Carboxypeptidase B, alpha-amylase, and alkaline phosphatase present in porcine small intestinal fluids did not cause a significant difference in sensitivity between virulent and attenuated virus isolates. The digestive enzymes: trypsin, alpha-chymotrypsin, pancreatin, peptidase, and carboxypeptidase A did not (or only slightly) inactivate virulent Miller strain TGE virus, but greatly reduced infectivity of attenuated viruses (Purdue strain and TGE vaccine virus isolates). The attenuated strains were significantly more sensitive to small intestinal fluids from both fasted and fed adult swine. Differential sensitivities between virulent and attenuated TGE viruses to digestive fluids from stomach and small intestine further substantiate the notion of differential susceptibility to small intestinal proteases as a correlate of viral virulence.
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PMID:Enzymatic and acidic sensitivity profiles of selected virulent and attenuated transmissible gastroenteritis viruses of swine. 298 96

In a series of 10 healthy pigs, the normal ranges of the following biochemical parameters in blood serum were assessed: creatinine, urea, mineralogram (Na, K, Cl), uric acid, bilirubin, total protein, cholesterol, blood lipid level, thymol turbidity reaction and activities of alkaline phosphatase, alpha-amylase and transaminases. The changes of these values were followed up in two pigs after bilateral nephrectomy and in 18 pigs subjected to orthotopic allotransplantation of the kidneys. The examination confirmed that creatinine and urea are the most important values with a prognostic impact. However, other biochemical values signalize also renal dysfunction. In the mineralogram, values of Na and K ions are important indicators. Deterioration of renal functions was associated as a rule with a decline of alpha-amylase and alkaline phosphatase. The other examinations did not display any marked changes during renal damage.
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PMID:Changes of clinical biochemical values after bilateral nephrectomy and allotransplantation of the kidney in pigs. 304 68

A DNA fragment from Bacillus natto IFO3936 has been cloned which enhances the production of both extracellular alkaline and neutral proteases in Bacillus subtilis. The DNA sequence analysis around the gene responsible for the hyperproduction, prtR, revealed one open reading frame (comprising 60 amino acid residues) which was bounded by potential transcriptional and translational regulatory signals in its preceding and following regions. This open reading frame was not homologous to the published sequences of the structural genes of the two proteases. The calculated molecular weight (7,109) of the polypeptide predicted from the DNA sequence is much smaller than those of the two proteases, indicating that the gene product is distinct from those enzymes. In-frame fusion between the N-terminal region of the coding sequence and the lacZ gene of Escherichia coli demonstrated that the coding region was indeed translated in vivo. By deletion analysis it was suggested that prtR was the structural gene for the 60-amino-acid polypeptide. Cells carrying a prtR plasmid secreted both proteases 40 to 400 times more than the cells carrying the vector alone. Furthermore, it was found that prtR also enhanced the production of levansucrase by 1 or 2 orders of magnitude. There was no difference, however, in the amount of the other extracellular enzymes such as alpha-amylase, RNase, and alkaline phosphatase. These results indicate that prtR is specific for the hyperproduction of the proteases and levansucrase.
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PMID:Molecular cloning and nucleotide sequence of a DNA fragment from Bacillus natto that enhances production of extracellular proteases and levansucrase in Bacillus subtilis. 308 53

Studies were performed on the prtR gene which enhances the production of the Bacillus subtilis extracellular proteases and levansucrase, but not the alpha-amylase, RNase, and alkaline phosphatase. To investigate the mode of action of prtR, the Escherichia coli bla gene was placed under the control of two promoters. One was the promoter of the alkaline protease gene (aprE), and the other was the promoter of B. subtilis dihydrofolate reductase gene (dfrA). Expression of the bla gene was enhanced by prtR only when the apr promoter was used. From these results, it was concluded that the apr promoter or its vicinity was the target of prtR and that prtR does not affect the process after transcription. The mRNA levels of aprE and nprE (the neutral protease gene) were significantly increased by prtR, but the half-life of the aprE mRNA was not affected. These results show that the prtR gene product enhances protease production by increasing the rate of transcription initiation.
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PMID:prtR enhances the mRNA level of the Bacillus subtilis extracellular proteases. 311 Jan 32

The Bacillus subtilis alpha-amylase structural gene (amyE) lacking its own signal peptide coding sequence was joined to the end of the Escherichia coli alkaline phosphatase (phoA) signal peptide coding sequence by using the technique of oligonucleotide-directed site-specific deletion. On induction of the phoA promoter, the B. subtilis alpha-amylase was expressed and almost all the activity was found in the periplasmic space of E. coli. The sequence of the five amino-terminal amino acids of the secreted polypeptide was Glu-Thr-Ala-Asn-Lys-, and thus the fused protein was correctly processed by the E. coli signal peptidase at the end of the phoA signal peptide.
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PMID:Secretion of Bacillus subtilis alpha-amylase in the periplasmic space of Escherichia coli. 311 69

We measured the relationship between measured activity concentration and temperature for alpha-amylase (EC 3.2.1.1), using 10 different substrates. At 25-37 degrees C the Arrhenius plot was linear. The activation energy ranged from 33.3 kJ.mol-1 with maltoheptaose as substrate to 54.4 kJ.mol-1 with the Blue-Starch method. Activation energy was lowest for substrates having seven glucose moieties, the ones most suitable for determining alpha-amylase--i.e., the presence of more or fewer glycosyl units increased the activation energy. Substrates with blocked groups at the nonreducing end of the oligosaccharide chain were not considered here, because the relative reaction rates obtained with these substrates were less than those obtained with nonblocked substrates. We also determined temperature-conversion factors for alpha-amylase reaction with the various substrates. The results are discussed in relation to thermodynamic parameters of some other enzymes, e.g., creatine kinase and alkaline phosphatase.
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PMID:Some thermodynamic parameters and temperature-conversion factors for determining alpha-amylase concentration in serum. 326 56

Biological intra-individual variation in the concentration of 15 biochemical analytes in serum was estimated for 17 patients with chronic renal failure (CRF) and compared with results for apparently healthy individuals. The ratio of the average intra-individual variation in CRF patients to that in normal subjects was 1.5 to 2.0 for sodium, chloride, calcium, and creatinine; 1.2 to 1.5 for hemoglobin, total protein, albumin, globulin, uric acid, cholesterol, and alpha-amylase. The intra-individual CVs for urea, high-density-lipoprotein cholesterol, triglycerides, and alkaline phosphatase did not differ significantly between groups. The intra-individual variation of calcium and the concentration of creatinine in serum correlate significantly (r = 0.661, p less than 0.01). Individual values showed a gaussian distribution for all analytes. There was no time dependence of the intra-individual variation during a three-week interval, except for calcium and cholesterol. The estimated biological component of intra-individual variation and the analytical variation can be used to derive decision-making criteria in monitoring CRF.
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PMID:Intra-individual variation of some analytes in serum of patients with chronic renal failure. 349 51

Alpha-amylase was present in considerable amount in the chyme in rats both at rest and during digestion, in the latter case its level being increased. Activity of intrinsic intestinal enzymes dominated in the homogenate of the mucosa. Transition from fasting to feeding and digestion increased the level of alkaline phosphatase and dipeptidase activities in the homogenate of the mucosa. The data obtained suggest the final stages of biopolymers' hydrolysis to be localized in various enterocyte structures. The surface mucus, owing to absorbed pancreatic enzymes, binding proteins and other types of physiologically active molecules, is assumed to play the role of a specific molecular filter and take part in the initial stages of digestion.
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PMID:[Radial and proximo-distal distribution of hydrolytic enzymes in the small intestine at rest and during digestion]. 366 10


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