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 three brush-border enzymes--alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), and gamma-glutamyltransferase (EC 2.3.2.2)--are present in the urine of healthy persons in two variants, a particulate form and a soluble one. They can be separated by electrophoresis in agarose gel and by ultracentrifugation. The particulate forms exhibit similar electrophoretic mobility, but the soluble forms of these brush-border enzymes differ in their electrophoretic mobilities. The enzyme components of the particulate activity can be mobilized by Triton X-100 and trypsin. The electrophoretic mobility of the soluble forms of alanine aminopeptidase and gamma-glutamyltransferase is slowed by neuraminidase treatment. Both forms of gamma-glutamyltransferase are influenced in their electrophoretic mobility by treatment with n-butanol/diisopropyl ether, showing their lipid dependence. These findings enhance our knowledge of the biochemical nature of brush-border enzymes in urine.
 ...
PMID:Electrophoretic variants of alanine aminopeptidase, alkaline phosphatase, and gamma-glutamyltransferase in urine. 614 5

Jejunal perfusion in the rat with Ringer solution containing 10 mmol/l taurocholate removes considerable quantities of protein and brush border membrane enzymes from the intestinal epithelium. The duration of the experiments was 7.5 h. One group of animals was given 200 micrograms cycloheximide per 100 g body weight intramuscularly 1 h before start of the perfusion. Serial estimations of protein and of four brush border membrane enzymes (alanine aminopeptidase, alkaline phosphatase, gamma-glutamyl transferase, and enteropeptidase) were done in the perfusate. The results provide evidence that during the experiments an increasing proportion of the enzymes stems from de novo synthesis. This is consistent with the concept that after loss of 10-30 per cent of enzyme the molecules are replaced by newly synthesized material, provided that the energy metabolism of the mucosa cells remains intact.
 ...
PMID:De novo synthesis of brush border membrane enzymes during intestinal perfusion with bile salt in the rat. 614 76

The catalytic activities of alanine aminopeptidase, alkaline phosphatase and gamma-glutamyltransferase were determined in the soluble and particulate fractions of urine, after ultracentrifugation. In healthy adults the fractional catalytic activities in the supernatants were 0.53, 0.56 and 0.24, respectively. Nearly the same proportions were found in children. In patients suffering from chronic kidney diseases there was a tendency for the proportion of catalytic activity in the soluble fraction to increase. However, the separation into the multiple forms gave no higher diagnostic reliability than the determination of total catalytic activity of the respective enzymes. The determination of multiple forms has no clinical significance in the detection of rejection episodes in renal transplant recipients.
 ...
PMID:Multiple forms of alanine aminopeptidase, alkaline phosphatase and gamma-glutamyltransferase in urine of healthy persons, patients suffering from kidney diseases and patients with kidney transplants. 614 52

The urinary brush-border enzymes alanine aminopeptidase, alkaline phosphatase and gamma-glutamyltransferase can be separated by ultracentrifugation into a particulate and a soluble fraction. These variants have been characterized with respect to their kinetic data, heat stability, electrophoretic mobility and behaviour in gel chromatography and affinity chromatography. Both variants of these enzymes show nearly identical Km values and activity curves as functions of rho H and substrate concentration. The particulate variant is more heat-sensitive than the soluble one. The soluble variant as well as the particulate form consist of one fraction bound by Con A-sepharose and another one unbound by it. Origins and nature of these multiple variants in connection with their possible diagnostic significance are discussed.
 ...
PMID:Characterization of particulate and soluble variants of the brush-border enzymes alanine aminopeptidase, alkaline phosphatase and gamma-glutamyltransferase in human urine. 615 36

Urinary excretion of the low molecular weight protein beta 2-microglobulin and tubular enzymes--alanine aminopeptidase (AAP), gamma-glutamyl transpeptidase (gamma-GT) and alkaline phosphatase (AP)--are very sensitive parameters for proximal tubular lesions. In patients with preeclampsia the renal excretion of beta 2-microglobulin allows to differentiate between a primary preeclampsia and a preeclampsia superimposed upon chronic pyelonephritis. In the first group the increase is 3- to 4-fold and in the second group up to 300-fold. In patients with kidney transplantation the urinary excretion of beta 2-microglobulin, AAP, gamma-GT and AP are several times higher than in normals. In case of a rejection episode a further increase of these proteins occur in more than 80% several days before clinical symptoms are present. The application of analgetics (paracetamol, acetylsalicylic acid) in healthy individuals in therapeutical dosages on 3 consecutive days does not show any tubular alteration by the measurement of urinary beta 2-microglobulin. Aminoglycosides (tobramycin, UK 18,892) lead to a cumulative increase of the renal excretion of beta 2-microglobulin and AAP while cephalosporins induce an increase of total proteins in the final urine under the same conditions.
 ...
PMID:Beta 2-microglobulin and other proteins as parameter for tubular function. 616 17

A survey of eleven enzyme activity levels in normal and SV40 transformed (VA-13) WI-38 cells revealed that the transformed cell enzymes differed by a quantitative and qualitative change of alkaline phosphatase and a quantitative loss of an arylamidase. Alkaline phosphatase activity was found to be elevated in the transformed cells at confluency but not in log phase cultures. This elevated activity was heat stable, L-homoarginine resistant and L-phenylalanine sensitive and is probably the term placental isoenzyme. In nontransformed WI-38 cells, the alkaline phosphatase was heat labile, L-homoarginine sensitive and L-phenylalanine resistant and so is probably the liver isoenzyme. While the arylamidase activity from both normal and transformed WI-38 cells had identical pH optima and Km values, the activity was approximately 20 times higher in confluent WI-38 cells than in confluent VA-13 cells. Cytochemical staining techniques for both activities are described that permit identification of fluorescent product within the cells, analysis of activity levels, and separation of cells with high and low activities. Mixtures of WI-38 cells and VA-13 cells separated by flow cytometry on the basis of arylamidase activity were subsequently evaluated for alkaline phosphatase isoenzyme and found to have been simultaneously separated into heat labile and heat stable samples.
 ...
PMID:Alkaline phosphatase and an acid arylamidase as marker enzymes for normal and transformed WI-38 cells. 624 91

Statistical analysis of variance was applied to data from determinations of 14 plasma constituents in 25 rats in order to evaluate the analytical, experimental and biological (inter-and intraindividual) component of variance. Blood was taken seven times in intervals of 8-10 days, the last one by catheter technique and the other by heart puncture. The analytical portion of variance was determined by the concurrent analysis of a pool plasma standard. The experimental component of variance was evaluated by the comparison of the variation of the catheter values with that of the pooled data from heart puncture. The coefficient of variation for the latter may be grouped into three categories: less than 10% for protein, Na+, K+, Ca2+; 10-20% for urea, phosphate and the enzymes as alanine aminotransferase, choline esterase, alkaline phosphatase and leucine arylamidase and 20-65% for the other enzymes lactate dehydrogenase, malate dehydrogenase, aspartate aminotransferase and creatine kinase. The results from the samples taken by catheter technique generally revealed the lower values for the mean as well as for the variance. It became evident that the procedure of heart puncture is afflicted with the most aggravating interference factors, thus accounting for most of the experimental component of variance. The observed differences between the single blood drawings, the non-Gaussian distribution for several constituents, and the interactions between the components of variance do not always fit for the statistical concept of additivity of the single components.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Biological, analytical and experimental components of variance in a long-term study of plasma constituents in rat. 660 70

Renal tissue sections from 178 patients, whose kidneys were either normal or altered by various conditions such as hydronephrosis, interstitial nephropathies, chronic graft rejection, renal cancer etc., were investigated by computer-assisted histophotometry. We used enzyme histochemical and immunologic methods to measure kidneys suffering from various urological diseases quantitatively. Through this procedure, we were able to obtain information that allowed us to determine the degree of alteration in the metabolic state of tubular epithelial cells. The tissue activities of the following enzymes of the proximal tubule were investigated: alanine aminopeptidase (AAP), alkaline phosphatase (AP) and maltase (Ma) as membrane-bound markers, and beta-glucuronidase (beta-Gl) as a lysosomal marker. In addition, AAP and gamma-glutamyltranspeptidase (GGTP) were measured by immunofluorescent microscopy after having added specific anti-enzyme antibodies to the tissue sections. Compared to normal kidneys, quantitative enzyme histograms of diseased kidneys revealed a significant decrease in marker protein concentration of the tubule. The decline in tissue enzyme activities of AP, AAP, Ma and beta-Gl was accompanied by a significant decrease of enzyme concentrations as measured by the immuno histological method. This was especially true in cases with kidney cancer and in kidney tissues adjacent to infiltration adenocarcinoma. Morphological analyses of alterations were generally improved by enzymatic and/or immunologic histophotometry.
 ...
PMID:Quantitative enzymatic and immunologic computer-assisted histophotometry of human kidney tissue following neoplastic and other clinically significant alterations. 687 27

The activity of alanine aminopeptidase, alkaline phosphatase, gamma-glutamyltransferase, lactate dehydrogenase and beta-N-acetyl-D-glucosaminidase in urine at 37 degrees C was investigated by a model simulating in vivo conditions. The stability of these urinary enzymes is influenced particularly by pH. At low pH values in urine (about pH 5.0) the four first-mentioned enzymes rapidly lose a considerable part of their activity, whereas beta-N-acetyl-D-glucosaminidase is inactivated at higher pH values in urine (about at pH 8.0). This inactivation effect is also time-dependent and can be modified by urinary substances such as creatinine, urea and electrolytes. To avoid misinterpretation of enzyme activity determinations in urine, the simultaneous measurement of urinary pH should be performed.
 ...
PMID:Stability of enzymes in urine at 37 degrees C. 688 14

During a long-term study in the rat some enzyme activities were determined in plasma, lung, spleen and skeletal muscle. Twelve rats of each sex were investigated every 49 days from 35 until 1115 days of life. Lactate dehydrogenase in lung and spleen decreases; in muscle and plasma, however, the activity varies considerably. Malate dehydrogenase in the tissues remains nearly unchanged apart from distinct peaks in the first year of life; in plasma the activity takes an M-shaped course. In contrast to the changes of glutamate dehydrogenase in the tissues with a tendency to diminish, this enzyme increases in plasma during the lifetime. Aspartate aminotransferase activity in the tissues, except muscle, varies with a rhythmical behaviour, and in plasma shows a gradual increase. Alanine aminotransferase in lung and spleen has two activity peaks. In muscle this enzyme varies only slightly after a steep initial decrease. In plasma the activity has a tendency to rise. Creatine kinase in the tissues reveals several activity peaks. In plasma the activity course is U-shaped. Adenylate kinase in spleen and lung rises, whereas in muscle the activity varies considerably. The nearly identical decrease of alkaline phosphatase activity in the tissues during ageing is also reflected by a concomitant behaviour in plasma. Leucine arylamidase in lung and muscle both have a U-shaped characteristic, whereas in spleen the activity changes in a shorter period. In plasma, a rhythmical behaviour is apparent. Aldolase in plasma tripled during the observation period. Except for lactate dehydrogenase and aldolase, distinct sex-differences are observed in plasma. With progressive age the animals suffer increasingly from characteristic diseases, which beside experimental components have influenced the enzyme pattern. Enzyme activities in plasma and tissues show a complex pattern and are only of limited importance in understanding the ageing process.
 ...
PMID:Long-term observation of plasma and tissue enzyme activities in the rat. 720 25


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>