Ab initioSCF study of the interaction betweenL-serine phosphate and ammonia

1989 ◽  
Vol 36 (5) ◽  
pp. 587-598
Author(s):  
Y. Nakamura ◽  
S. Lunell
Keyword(s):  
Serine Phosphate

scholarly journals Turnover of protein-bound serine phosphate in respiring slices of guinea-pig cerebral cortex. Effects of putative transmitters, tetrodotoxin and other agents

1973 ◽  
Vol 132 (3) ◽  
pp. 475-482 ◽  
Author(s):  
Martin Reddington ◽  
Richard Rodnight ◽  
Michael Williams
Keyword(s):  
Cerebral Cortex ◽  
Cyclic Amp ◽  
Guinea Pig ◽  
Electrical Pulses ◽  
Phosphorus Turnover ◽  
Serine Phosphate ◽  
Stimulation Of

1. The effect of various agents on the turnover of protein-bound phosphorus in respiring slices of cerebral cortex was studied. 2. Confirming previous work turnover was increased by the application of electrical pulses for 10s to the tissue. 3. Turnover was also increased by exposure of the slices for 10min to noradrenaline (0.5mm), 5-hydroxytryptamine (1μm) and histamine (0.1mm). 4. When slices were stimulated by electrical pulses in the presence of histamine the increase in turnover was the sum of the responses given by each agent above, suggesting that different phosphorylating systems were involved. 5. Tetrodotoxin (0.5μm) blocked the increased turnover due to electrical pulses, but not that due to histamine. Tetrodotoxin also prevented the increase in tissue cyclic AMP content caused by the application of electrical pulses. 6. Phosphoprotein turnover was not affected by adenosine, despite the increase in tissue cyclic AMP content given by this agent. 7. Adenosine blocked the phosphoprotein response to histamine, but did not affect the response to electrical pulses. 8. The results are discussed in relation to the hypothesis that the stimulation of protein phosphorus turnover by electrical pulses is secondary to the release of cyclic AMP in the tissue.

Crystal Structure of L-Serine Phosphate

Nature ◽  
1959 ◽  
Vol 184 (4702) ◽  
pp. 1863-1864 ◽  
Author(s):  
G. H. McCALLUM ◽  
J. MONTEATH ROBERTSON ◽  
G. A. SIM
Keyword(s):  
Crystal Structure ◽  
Serine Phosphate

Crystal structure of L-serine phosphate

2005 ◽  
Vol 50 (1) ◽  
pp. 58-60 ◽  
Author(s):  
Yu. I. Smolin ◽  
A. E. Lapshin ◽  
G. A. Pankova
Keyword(s):  
Crystal Structure ◽  
Serine Phosphate

Crystal structure of di-(L-serine) phosphate monohydrate [C3O3NH7]2H3PO4H2O

2003 ◽  
Vol 45 (10) ◽  
pp. 1893-1897 ◽  
Author(s):  
Yu. I. Smolin ◽  
A. E. Lapshin ◽  
G. A. Pankova
Keyword(s):  
Crystal Structure ◽  
Serine Phosphate

CONCERNING THE NATURE OF THE α- AND β-LYTIC PROTEASES OF SORANGIUM SP.

1967 ◽  
Vol 45 (6) ◽  
pp. 911-916 ◽  
Author(s):  
D. R. Whitaker ◽  
C. Roy
Keyword(s):  
Amino Acid ◽  
Serine Protease ◽  
Lytic Enzyme ◽  
Serine Residue ◽  
Terminal Amino Acid ◽  
Electrophoretic Patterns ◽  
Diisopropyl Phosphorofluoridate ◽  
Terminal Amino ◽  
Inhibited Enzyme ◽  
Serine Phosphate

The α-lytic protease is readily inhibited by diisopropyl phosphorofluoridate (DFP) and the yield of serine phosphate from acid-hydrolyzed, DFP-inhibited enzyme indicates that DFP esterifies one serine residue of the enzyme. Acid digests of enzyme treated with isopropyl methylphosphonofluoridate-32P (sarin) show much the same electrophoretic patterns of 32P-labelled peptides as similar digests of sarin-treated trypsin and chymotrypsin; amino acid analyses and N-terminal amino acid analyses of peptides isolated from the digest confirm that the α-enzyme has the same sequence (Asp-Ser*-Gly-Gly) around the reactive serine residue as the pancreatic enzymes. At present, the α-enzyme is the only microbial "serine protease" which is known to have this sequence. It is also unique as a serine protease in that it has only one histidine residue.The β-lytic enzyme is not inhibited by DFP and shows no evidence of reactivity towards sarin. Its zinc atom can be removed by o-phenanthroline without loss of lytic activity. At present, it cannot be classed in any of the major groups of proteases.

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