Alkaline Phosphatases
Mostrando 13-24 de 100 artigos, teses e dissertações.
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13. Alkaline phosphatase of mouse teratoma stem cells: Immunochemical and structural evidence for its identity as a somatic gene product
The immunochemical and structural characteristics of the alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] from mouse teratoma stem cells derived from the OTT-6050 teratoma (ascitic and solid tumors and the F9 and PCC4 cell lines) have been compared to those of the alkaline phosphatases expressed in normal mouse
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14. Biochemical characterization of the extracellular phosphatases produced by phosphorus-deprived Chlamydomonas reinhardtii.
We have examined the extracellular phosphatases produced by the terrestrial green alga Chlamydomonas reinhardtii in response to phosphorus deprivation. Phosphorus-deprived cells increase extra-cellular alkaline phosphatase activity 300-fold relative to unstarved cells. The alkaline phosphatases are released into the medium by cell-wall-deficient strains and
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15. Partial sequencing of human adult, human fetal, and bovine intestinal alkaline phosphatases: comparison with the human placental and liver isozymes.
Purification, molecular weights, amino acid compositions, and partial sequencing of intestinal alkaline phosphatases (EC 3.1.3.1) from human adult, human fetal, and bovine sources is reported. Additional sequence information is presented for the bovine liver isozyme. Comparisons are made of the partial primary structures of intestinal alkaline phosphatases w
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16. Electrophoretic separation of tissue-specific serum alkaline phosphatases
Previous electrophoretic methods for the separation of tissue-specific serum alkaline phosphatases have either been unable to separate the liver and bone enzymes or have been too involved for routine clinical use. A relatively simple electrophoretic method is described which separates placental, liver, bone, and intestinal alkaline phosphatases in serum. The
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17. Expression of alkaline phosphatase loci in mammalian tissues
Alkaline phosphatases [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] have been examined in liver, bone, kidney, intestine, and placenta from nine mammalian species by quantitative inhibition and thermostability studies and compared with alkaline phosphatases in the corresponding human tissues. In humans, three kinds of alkaline p
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18. Enzyme Evolution in the Enterobacteriaceae1
An immunological approach has been used for the study of alkaline phosphatase evolution in bacteria of the family Enterobacteriaceae. Antisera were prepared against alkaline phosphatase from Escherichia coli and Klebsiella aerogenes and tested against the unpurified alkaline phosphatases of 32 strains of enterobacteria by double diffusion and quantitative mi
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19. Serum alkaline phosphatase fractionation as an aid to diagnosis
A case is reported in which the serum alkaline phosphatase reached high levels, and in which the differential diagnosis between hepatic secondary deposits and osteomalacia proved difficult by the usual means. Separation of the alkaline phosphatases by starch grain electrophoresis was used as an aid to differential diagnosis.
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20. Human Alkaline Phosphatases. Progress in Clinical and Biological Research
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21. Developmental change in human intestinal alkaline phosphatase.
Starch gel electrophoresis and inhibition studies with L-phenylalanine, L-homoarginine, L-leucine, L-leucylglycylglycine, and L-phenylalanylglycylglycine were carried out on a series of human alkaline phosphatases [orthophosphoric-monoester phosphohydrolase (alkaline optimum); EC 3.1.3.1] derived from fetal and adult liver, kidney, bone, and intestine. No di
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22. Identification of a Regulated Alkaline Phosphatase, a Cell Surface-Associated Lipoprotein, in Mycobacterium smegmatis
Although alkaline phosphatases are common in a wide variety of bacteria, there has been no prior evidence for alkaline phosphatases in Mycobacterium smegmatis. Here we report that transposon insertions in the pst operon, encoding homologues of an inorganic phosphate transporter, leads to constitutive expression of a protein with alkaline phosphatase activity
American Society for Microbiology.
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23. Phosphatase of Chlamydomonas reinhardi: biochemical and cytochemical approach with specific mutants.
The unicellular alga Chlamydomonas reinhardi produces two constitutive acid phosphatases and three depressible phosphatases (a neutral and two alkaline ones) that can utilize napthyl phosphate as a substrate. Specific mutants depressible phosphatase were used to investigate biochemical properties and the cytochemical localization of these enzymes. The two co
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24. The phosphatases of peripheral white blood cells in workers exposed to trichloroethylene and perchloroethylene
Friborská, A. (1969).Brit. J. industr. Med.,26, 159-161. The phosphatases of peripheral white blood cells in workers exposed to trichloroethylene and perchloroethylene. The activity of leucocyte alkaline phosphatase was found to be increased in people continuously exposed during their working hours to trichloroethylene. The increase correlated with the seve