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Characterization of alkaline phosphatase and organic phosphorous utilization in the oceanic dinoflagellate Pyrocystis noctiluca

Characterization of alkaline phosphatase and organic phosphorous utilization in the oceanic... 227 61 61 1 1 R. B. Rivkin E. Swift Graduate School of Oceanography University of Rhode Island 02881 Kingston RI USA Department of Botany University of Rhode Island 02881 Kingston RI USA Department of Biology and McCollum Pratt Institute The Johns Hopkins University 21218 Baltimore MD USA Abstract Phosphate depleted Pyrocystis noctiluca (Murray) Schuett 1895 has at least one phosphomonoesterase (EC 3:1:3:1) which is triphasic between 0.1 and 222 μmol P. The enzyme has a broad temperature range with maximum activity at 50 °C and a Q 10 of 1.4 to 1.5. A break in the Arrhenius plot at 35 °C implies the enzyme is membrane-bound. Cytological staining of whole cells and cell fractionation studies (showing 26 times higher specific activity in the particulate compared with the cytoplasmic fraction) suggest the enzyme is plasmalemma-bound. The enzyme has an absolute metal requirement which would be satisfied by Mg ++ but not Mn ++ , Zn ++ , Fe ++ , or Co ++ at seawater concentrations. Alkaline phosphatase is a stable enzyme whose activity is not altered by inhibitors of protein synthesis. Orthophosphate inhibition of enzyme activity was largely eliminated in the presence of these inhibitors. Apparently, a protein induced by PO 4 3- , rather than PO 4 3- itself, inhibits alkaline phosphatase. Cell-free alkaline phosphatase can hydrolyze a variety of phosphate esters and linear polymers of inorganic phosphorus as well as disolved organic phosphorus from tropical oceanic waters. These same hydrolysable organic and inorganic phosphorus compounds support the axenic culture growth of P. noctiluca , suggesting that naturally occurring hydrolysable organic phosphorus compounds may also support the growth of this alga. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Marine Biology Springer Journals

Characterization of alkaline phosphatase and organic phosphorous utilization in the oceanic dinoflagellate Pyrocystis noctiluca

Marine Biology , Volume 61 (1) – Dec 1, 1980

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References (49)

Publisher
Springer Journals
Copyright
Copyright © 1980 by Springer-Verlag
Subject
Life Sciences; Biomedicine general; Oceanography; Ecology; Microbiology; Zoology
ISSN
0025-3162
eISSN
1432-1793
DOI
10.1007/BF00410336
Publisher site
See Article on Publisher Site

Abstract

227 61 61 1 1 R. B. Rivkin E. Swift Graduate School of Oceanography University of Rhode Island 02881 Kingston RI USA Department of Botany University of Rhode Island 02881 Kingston RI USA Department of Biology and McCollum Pratt Institute The Johns Hopkins University 21218 Baltimore MD USA Abstract Phosphate depleted Pyrocystis noctiluca (Murray) Schuett 1895 has at least one phosphomonoesterase (EC 3:1:3:1) which is triphasic between 0.1 and 222 μmol P. The enzyme has a broad temperature range with maximum activity at 50 °C and a Q 10 of 1.4 to 1.5. A break in the Arrhenius plot at 35 °C implies the enzyme is membrane-bound. Cytological staining of whole cells and cell fractionation studies (showing 26 times higher specific activity in the particulate compared with the cytoplasmic fraction) suggest the enzyme is plasmalemma-bound. The enzyme has an absolute metal requirement which would be satisfied by Mg ++ but not Mn ++ , Zn ++ , Fe ++ , or Co ++ at seawater concentrations. Alkaline phosphatase is a stable enzyme whose activity is not altered by inhibitors of protein synthesis. Orthophosphate inhibition of enzyme activity was largely eliminated in the presence of these inhibitors. Apparently, a protein induced by PO 4 3- , rather than PO 4 3- itself, inhibits alkaline phosphatase. Cell-free alkaline phosphatase can hydrolyze a variety of phosphate esters and linear polymers of inorganic phosphorus as well as disolved organic phosphorus from tropical oceanic waters. These same hydrolysable organic and inorganic phosphorus compounds support the axenic culture growth of P. noctiluca , suggesting that naturally occurring hydrolysable organic phosphorus compounds may also support the growth of this alga.

Journal

Marine BiologySpringer Journals

Published: Dec 1, 1980

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