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)

Brush border (BB) membranes, isolated from human kidney cortex by density gradient centrifugation, revealed a distinct pattern of structural proteins as could be shown by bio- and immunochemical studies. Marker enzymes such as gamma-glutamyltranspeptidase (GGTP) and alanine-aminopeptidase (AAP) were characterized as extrinsic; alkaline phosphatase (AP) was characterized as an integral constituent of the BB membrane. The surface of the BB membranes exhibited numerous 5 nm particles bound through a linear component to the peripheral BB matrix (negative staining). Increase of AAP and GGTP (30%) activity in the supernatant after proteolytic treatment of BB fragments paralleled selective release of these constituents from the membranes. The surface components were found to be part of BB concanavalin A and wheat germ agglutinin receptor sites. Labelled antisera directed against surface glycoprotein fractions gave a specific immuno fluorescence staining of only the luminal plasma-membrane from the proximal tubule epithelia.
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PMID:Biochemical, immunological and ultrastructural studies on brush-border membranes of human kidney. 2 5

5'-Nucleotidase, assayed as 5'-AMPase, has been extensively characterized and established as a stable, quantitative plasma membrane marker in HeLa S3 cells. The membrane 5'-AMPase has a Km of 7.0 microM. Relative affinities of the other 5'-mononucleotides for the enzyme are 5'-GMP > 5'-TMP > 5'-UMP > 5'-CMP. There are activity optima at pH7 and 10; the latter is Mg(2+)-dependent. The membrane preparations have a small amount of acid phosphatase activity that is distinct from 5'-AMPase activity but no alkaline phosphatase. AOPCP, ADP, and ATP are strongly inhibitory. Mg2+, Ca2+, or Co2+ additions do not affect the pH 7.0 activity; Mn2+ activates slightly, whereas Zn2+, Cu2+, and Ni2+ are inhibitory. EDTA slowly inactivates, but removal of the EDTA without the addition of divalent cations restores activity. The inactivation is also substantially reversed by Co2+ or Mn2+, but reactivability by divalent cations decreases with time in EDTA. ConA strongly inhibits, and alpha-methyl-D-mannoside or glucose (the latter much less efficiently) relieves the inhibition, indicating that the 5'-AMPase is a glycoprotein. Histidine is also inhibitory. Ouabain, phloretin, cytochalasin B, cysteine, phenyl-alanine, MalNEt, and IAA are without effect. 5'-AMPase activity codistributes with pulse-bound [3H]ouabain when either of two cell fractionation procedures are used. The 5'-AMPase activity per cell is constant at different cell densities in exponentially growing cells, and activity per unit cell volume remains constant throughout the cell cycle. These properties, together with its absence in other organelles, its stability to storage, its insensitivity to certain experimental manipulations, and its general insensitivity to inhibitors of specific transport systems, make 5'-AMPase a useful quantitative marker in studies on the regulation of HeLa membrane transport systems. Key Words: HeLa, 5'-nucleotidase, plasma membrane marker, non-specific phosphatases, divalent ions, ConA, AOPCP, cell cycle, mitochondria, transport inhibitors.
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PMID:Characterization of HeLa 5'-nucleotidase: a stable plasma membrane marker. 4 80

1) Variations in the serum concentrations of total proteins and the electrophoretic fractions, glycoprotein, mucoprotein, fibrinogen, erythrocyte sedimentation rate, calcium, phosphorus, alkaline, and acid phosphatases were analyzed until the 30th day following uncomplicated fracture of shafts of long bones of the limbs in 25 cases. 2) A significant fall of albumin with concomitant rise of alpha 1, alpha 2, and beta globulins were noted until 30th day. 3) Mucoprotein, glycoprotein, and fibrinogen showed parallel elevations with that of alpha and beta globulins. 4) The peak values of alpha 1 and alpha 2 globulins, mucoprotein, and fibrinogen were registered on the 10th day after trauma. Albumin showed maximum fall on the 10th day in all these cases. 5) Glycoprotein showed a peak value on the 5th day. 6) Total protein and gamma globulin remained almost unchanged throughout the studies. 7) Beta globulin showed higher values and paralleled more closely the fibrinogen and erythrocyte sedementation rates. 8) The elevations of beta globulin, fibrinogen, and erythrocyte sedimentation rate were higher, and persisted beyond 30 days in lower-limb fractures as compared to upper-limb fractures. 9) Serum calcium, phosphorus, alkaline phosphatase, and acid phosphatase were not significantly different following fractures and therefore did not reflect much physiologic variation. 10) The most significant changes in the levels of plasma fractions studied were conspicuous on the 10th day and lasted for about 1 month.
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PMID:Variations of some plasma components after closed fractures. 5 53

Nineteen biochemical parameters, most of which have been individually advocated as tumour-index-substances for breast cancer, were measured in 51 patients with breast disease, 42 of whom had active breast cancer. Seven of these parameters were raised in more than half of the 17 patients of the series with overt metastases; these were serum ferritin (88%), C-reactive protein (87%), carcinoembryonic antigen (81%), acid glycoprotein (75%), total alkaline phosphatase (64%), sialyl transferase (56%), andthe urinary hydroxyproline/creatinine ratio (73%). The incidence of biochemical abnormalities in patients in this group compared favourably with the results of physical methods of detecting metastases. 7 of 16 further patients without evidence of distant metastases, but who had a poor prognosis as judged by histology of the primary tumour and axillary lymph-nodes, had abnormalities of at least one of the seven parameters. 3 of these patients have relapsed within a year of mastectomy. The results suggest that these biochemical tests could assist in monitoring metastatic disease and could indicate at the time of mastectomy, patients who might benefit from immediate systemic therapy in addition to local treatment of their breast carcinomas.
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PMID:Biochemical markers in human breast cancer. 6 63

Proteins, which are elevated in their blood concentration in pregnant women and patients suffering from malignant tumours, are reported because of their growing significance for the clinical practice. At present mainly are the following "pregnancy" proteins of clinical relevance: human chorionic gonadotrophin (HCG), human placental lactogen (HPL), placental heatstable alkaline phosphatase (HAP), pegnancy-associated alpha2-glycoprotein ("pregnancy zone" protein, PZ), socalled pregnancy-specific beta1-glycoprotein (SP1) and alpha1-fetoprotein (AFP). Applications to the clinical practice may be the surveillance of normal pregnancy, the recognition of dangerous conditions for mother and fetus, the inhibition of graft rejection, the induction of abortion, antibodies against pregnancy proteins as abortifacient and antifertilizer as well as the tumour diagnosis including the control of treatment and recognition of recidives.
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PMID:[Pregnancy proteins]. 7 23

The Ca2+-binding glycoprotein isolated from preosseous cartilage shows also alkaline phosphatase activity. The purification procedure indicates that the enzyme is inhibited in crude extract and conceivably in the intact tissue; the activity may be controlled by the proteoglycans present in the matrix. Other substrates are hydrolyzed by the purified enzyme in addition to p-nitrophenylphosphate; the highest specific activity was measured with ATP and pyrophosphate (PPi) at pH 7.5 and 9.0 Mg2+ induces an activation of ATP and PPi hydrolysis; Ca2+ activates hydrolysis of ATP but inhibits that of PPi. The glycoprotein shows also transphosphorylase activity, L-serine being the best phosphate acceptor. The release or transfer of Pi catalyzed by the glycoprotein can be an important step in calcium phosphate precipitation.
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PMID:Enzymatic properties of the Ca2+-binding glycoprotein isolated from preosseous cartilage. 11 41

1. Six rat liver plasma-membrane subfractions of different density and morphological, enzymic and chemical properties were prepared from homogenates by a combination of differential, rate-zonal and density-gradient centrifugation. They consisted of three vesicular 'light' subfractions of density 1.12-1.13 and three 'heavy' subfractions of density 1.16-1.18 containing membrane strips and intercellular junctions. 2. All six subfractions contained a basal adenylate cyclase activity. One of the 'light' subfractions that showed the highest glucagon-stimulated adenylate cyclase activity was identified as deriving form the blood-sinusoidal face of the hepatocyte. This subfraction, unlike the others, was contaminated by Golgi components, as indicated by its morphological properties and the presence of galactosyl- and sialyl-transferase activities. 3. All the six subfractions showed high activities of the following plasma-membrane marker enzymes: 5'-nucleotidase, alkaline phosphodiesterase (nucleotide pyrophosphatase), alkaline phosphatase, leucine naphthylamidase and Mg2+-activated adenosine triphosphatase. A 'light' subfraction that showed the highest specific activities of all the above marker enzymes, but lacked a glucagon-stimulated adenylate cyclase activity, was identified as deriving from the bile-canalicular face of the hepatocyte. 4. The 'heavy' subfractions, which showed generally the lowest activities of the above plasma-membrane enzyme markers, and were characterized by the presence of desmosomes and gap junctions, were taken to originate from the contiguous faces of the hepatocyte. 5. The protein composition of the six subfractions was generally similar, as shown by polyacrylamide-gel electrophoresis. Differences in the amounts of various protein and glycoprotein bands among the subfractions correlated with their morphology, enzymic composition and sialic acid content. 6. Hormonal and histochemical evidence supporting the identification of a bile-canalicular subfraction, a blood-sinusoidal subfraction and contiguous-face subfractions is discussed.
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PMID:Functional polarity of the rat hepatocyte surface membrane. Isolation and characterization of plasma-membrane subfractions from the blood-sinusoidal, bile-Canalicular and contiguous surfaces of the hepatocyte. 12 84

The main components of the schistome tegument were found to be neutral glycoprotein and phospholipid; a small quantity of glycolipid was observed in the male dorsal tegument. The tegument can be differentiated from other schisotsome tissues on the basis of enzyme content; three hydrolytic enzymes were shown to be specifically localized in the tegument: alkaline phosphatase, adenosine triphosphatase and indoxyl esterase. It is suggested that these enzymes could be used as intrinsic markers for tegument structures. The subtegumental cells appear to be the major sites of biosynthetic activity since they contain large amounts of RNA and mitochondrial enzymes.
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PMID:The tegument of Schistosoma mansoni: a histochemical investigation. 13 Jun 8

5 serum protein polymorphic systems (haptoglobin, alkaline phosphatase, group-specific (Gc) proteins, beta2-glycoprotein 1 and leucine aminopeptidase) and 6 red-cell polymorphisms (adenosine deaminase, adenylate kinase, phosphoglucomutase, glutamic-pyruvic transaminase, phosphogluconate dehydrogenase and acid phosphatase) have been investigated in 54 subjects with tuberous sclerosis. The frequencies of all systems were compared with those of a control sample drawn from a similar mentally retarded population and abnormal distributions were detected in the haptoglobin and Gc system. Quantitative estimation of the serum levels of the Gc protein failed to detect any inter-group differences. Data on the deviations from the Hardy-Weinberg equlibrium, Haldane's Log ratio test between groups, and gene frequencies of both test and control groups are given. It is suggested that selection by mortality is the possible causation for the abnormal distribution of the Gc phenotypes, but the haptoglobin phenotype distribution requires further investigation with care being taken in the selection of control subjects.
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PMID:Serum and tissue proteins in tuberous sclerosis. I. Serum and red-cell polymorphic systems. 16 11

Human placenta alkaline phosphatase (HP-ALP), a glycoprotein, was stained histochemically for the purpose of examining the concanavalin A (Con A) binding sites on the cell surface. HP-ALP was bound to the cell surface by Con A. This simple method successfully detected Con A binding sites on the cell surface.
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PMID:A new histochemical method using human placenta alkaline phosphatase for demonstrating concanavalin A binding sites on cell surfaces. 18 Jul 55


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