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Alkaline phosphatase

About: Alkaline phosphatase is a research topic. Over the lifetime, 20218 publications have been published within this topic receiving 540547 citations. The topic is also known as: Alkaline_phosphatase & IPR001952.


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Journal ArticleDOI
TL;DR: It was demonstrated for the first time that MSCs immobilized in this 3D matrix were able to enhance the ability of neighboring endothelial cells to form tubelike structures, which represents a step forward in the development of injectable stem cell carriers for bone tissue engineering.

142 citations

Journal ArticleDOI
TL;DR: "I Yanofsky, C., and P. R. Maling, Cellular Regulatory Mechanisms, Cold Spring Harbor Symposia on Quantitative Biology, vol.
Abstract: I Yanofsky, C., and P. St. Lawrence, Ann. Rev. Microbiol., 14, 311 (1960). 16 Yanofsky, C., D. R. Helinski, and B. Maling, in Cellular Regulatory Mechanisms, Cold Spring Harbor Symposia on Quantitative Biology, vol. 26 (1961), p. 11. 17 Hoagland, M. B., Brookhaven Symposia in Biol., 12, 40 (1959). 18 Crick, F. H. C., "The Biological Replication of Macromolecules," in Symposium Soc. Expt. Biol., 12, 138 (1958). 19 Chapeville, F., F. Lipmann, G. von Ehrenstein, B. Weisblum, W. Ray, and S. Benzer, these PROCEEDINGS, 48, 1086 (1962). 20 von Ehrenstein, G., and F. Lipmann, these PROCEEDINGS, 47, 941 (1961). 21 Nomura, M., and S. Benzer, J. Mol. Biol., 3, 684 (1961). 22 Bode, W., doctoral dissertation, University of Cologne (1962). 23 Weisblum, B., S. Benzer, and R. Holley, manuscript in preparation. 24 Benzer, S., and B. Weisblum, these PROCEEDINGS, 47, 1149 (1961).

142 citations

Journal ArticleDOI
TL;DR: It is demonstrated that an active enzyme can be expressed on the surface of a bacteriophage and the functional enzyme is co-purified with the DNA encoding it, which may permit a novel approach to enzyme engineering based on affinity chromatography of mutant enzymes expressing on the phage surface.
Abstract: We have demonstrated that an active enzyme can be expressed on the surface of a bacteriophage. The gene encoding alkaline phosphatase from Escherichia coli was cloned upstream of gene 3, which encodes a minor coat protein of the filamentous bacteriophage, fd. A fusion protein of the correct size was detected from viral particles by Western blotting. Ultrafiltration confirmed that the enzyme fusion behaves as part of a larger structure as would be expected of an enzyme fused to a viral particle. Both wild-type alkaline phosphatase (Arg166) and an active site mutant (Ala166) expressed in this way retain catalytic activity and have qualitatively similar kinetic properties to free enzyme. Values were obtained for Km of 72.7 and 1070 microM respectively whilst relative kcat for the mutant was 36% of that for wild-type. Phage particles expressing alkaline phosphatase were bound to an immobilized inhibitor (arsenate-Sepharose) and eluted with product (20 mM inorganic phosphate). In this way, the functional enzyme is co-purified with the DNA encoding it. This may permit a novel approach to enzyme engineering based on affinity chromatography of mutant enzymes expressed on the phage surface.

142 citations

Journal ArticleDOI
01 Jan 1990-Bone
TL;DR: It is suggested that by regulating local production of growth factors such as IGF-1, GH and 1,25(OH)2D3 may modulate the metabolism of human bone cells.

141 citations

Journal ArticleDOI
TL;DR: Increased hydrolysis of PP(i) by tissue-nonspecific alkaline phosphatase (TNAP) may occur in renal failure and act to enhance mineralization of vessels.

141 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20241
2023795
20221,761
2021271
2020302
2019294