THE BIOCHEMISTRY OF THE NITRIFYING ORGANISMS: PART 7. THE PHOSPHATE COMPOUNDS OF NITROBACTER AND THE UPTAKE OF ORTHOPHOSPHATE BY THE ORGANISM

1960 ◽  
Vol 38 (1) ◽  
pp. 1295-1300 ◽  
Author(s):  
W. D. Butt ◽  
H. Lees
Keyword(s):  
Slow Rate ◽  
Total Cell ◽  
Nitrite Oxidation ◽  
Trichloracetic Acid ◽  
Alkali Extract ◽  
Labile Component ◽  
Autotrophic Bacterium ◽  
Acid Labile ◽  
Labile Compound ◽  
Phosphate Compounds

The phosphate compounds present in the cells of the chemosynthetic autotrophic bacterium Nitrobacter were fractionated by means of successive extractions with cold 5% trichloracetic acid, ethanol, ethanol:ether, and dilute alkali. It was found that about 50% of the total cell phosphate was soluble in dilute alkali and, of this, 76% was acid-labile. Treatment of the alkali extract with Norit reduced the content of non-labile phosphate without affecting the acid-labile component; this labile compound was identified as a polyphosphate. By the use of 32P-labelled orthophosphate, it was shown that the cells absorbed orthophosphate from the medium at a slow rate during nitrite oxidation.

THE BIOCHEMISTRY OF THE NITRIFYING ORGANISMS: PART 7. THE PHOSPHATE COMPOUNDS OF NITROBACTER AND THE UPTAKE OF ORTHOPHOSPHATE BY THE ORGANISM

1960 ◽  
Vol 38 (11) ◽  
pp. 1295-1300
Author(s):  
W. D. Butt ◽  
H. Lees
Keyword(s):  
Slow Rate ◽  
Total Cell ◽  
Nitrite Oxidation ◽  
Trichloracetic Acid ◽  
Alkali Extract ◽  
Labile Component ◽  
Autotrophic Bacterium ◽  
Acid Labile ◽  
Labile Compound ◽  
Phosphate Compounds

The phosphate compounds present in the cells of the chemosynthetic autotrophic bacterium Nitrobacter were fractionated by means of successive extractions with cold 5% trichloracetic acid, ethanol, ethanol:ether, and dilute alkali. It was found that about 50% of the total cell phosphate was soluble in dilute alkali and, of this, 76% was acid-labile. Treatment of the alkali extract with Norit reduced the content of non-labile phosphate without affecting the acid-labile component; this labile compound was identified as a polyphosphate. By the use of 32P-labelled orthophosphate, it was shown that the cells absorbed orthophosphate from the medium at a slow rate during nitrite oxidation.

scholarly journals Membrane traffic in animal cells: cellular glycoproteins return to the site of Golgi mannosidase I.

1986 ◽  
Vol 103 (1) ◽  
pp. 265-275 ◽  
Author(s):  
M D Snider ◽  
O C Rogers
Keyword(s):  
Golgi Complex ◽  
Transferrin Receptor ◽  
Slow Rate ◽  
De Novo ◽  
Total Cell ◽  
Reversible Inhibitor ◽  
Oligosaccharide Synthesis ◽  
Animal Cells ◽  
Glycoprotein Synthesis ◽  
Erythroleukemia Cells

The recycling of cellular glycoproteins to the site of Golgi mannosidase I, an enzyme of asparagine-linked oligosaccharide synthesis, was studied in K562 human erythroleukemia cells. Cells were metabolically labeled in the presence of deoxymannojirimycin, a reversible inhibitor of Golgi mannosidase I. This generates glycoproteins with immature oligosaccharides in their normal locations. Transport to the mannosidase I compartment was then assessed by testing for the conversion of oligosaccharides into mature forms during reculture without deoxymannojirimycin. Transferrin receptor (TfR) was acted on by mannosidase I during reculture, suggesting that it returned to the region of the Golgi complex where this enzyme resides. The slow rate of this transport (t1/2 greater than 6 h) implies that it is probably different than TfR movement during transferrin internalization (t1/2 = 10-20 min) and TfR transport to the sialyltransferase compartment in the Golgi complex (t1/2 = 2-3 h) (Snider, M. D., and O. C. Rogers, 1985, J. Cell Biol., 100:826-834). The total cell glycoprotein pool was also transported to the mannosidase I compartment with a half-time of 4 h. Because this transport is 5-10 times faster than the rate of de novo glycoprotein synthesis in these cells, it is likely that most of the glycoprotein traffic through the Golgi complex is composed of recycling molecules.

Trichloracetic Acid-Insoluble Phosphate Compounds in Cartilage

Nature ◽  
1959 ◽  
Vol 183 (4665) ◽  
pp. 876-877 ◽  
Author(s):  
R. G. WHITEHEAD ◽  
S. M. WEIDMANN
Keyword(s):  
Trichloracetic Acid ◽  
Insoluble Phosphate ◽  
Phosphate Compounds

Rapid and reliable preparation of total cell lysates from fission yeast

2006 ◽  
Author(s):  
Atsuko Shirai ◽  
Akihisa Matsuyama ◽  
Yoko Yashiroda ◽  
Ritsuko Arai ◽  
Minoru Yoshida
Keyword(s):  
Fission Yeast ◽  
Total Cell ◽  
Cell Lysates

Concise Synthesis of GB22 by Endo-Selective Siloxycyclopropane Arylation

2019 ◽  
Author(s):  
Hannah E. Burdge ◽  
Takuya Oguma ◽  
Takahiro Kawajiri ◽  
Ryan Shenvi
Keyword(s):  
Intramolecular Cyclization ◽  
Cross Coupling ◽  
Building Blocks ◽  
Ring Expansion ◽  
Dual Catalysis ◽  
Acid Labile

<div><div><div><p>The first synthesis of GB22 was accomplished by a con- cise, modular route. Two building blocks converged in a novel sp3-sp2 attached-ring coupling that used Ir/Ni dual-catalysis to reverse the regioselectivity of siloxycy- clopropane arylation. This cross-coupling proved general to access β-substituted tetralones via ring-expansion of indanone-derived siloxycyclopropanes. The congested, bridging rings of the GB alkaloids were completed using an aluminum-HFIP complex that effected intramolecular cyclization of an acid-labile substrate.</p></div></div></div>

Concise Synthesis of GB22 by Endo-Selective Siloxycyclopropane Arylation

2019 ◽  
Author(s):  
Hannah E. Burdge ◽  
Takuya Oguma ◽  
Takahiro Kawajiri ◽  
Ryan Shenvi
Keyword(s):  
Intramolecular Cyclization ◽  
Cross Coupling ◽  
Building Blocks ◽  
Ring Expansion ◽  
Dual Catalysis ◽  
Acid Labile

<div><div><div><p>The first synthesis of GB22 was accomplished by a con- cise, modular route. Two building blocks converged in a novel sp3-sp2 attached-ring coupling that used Ir/Ni dual-catalysis to reverse the regioselectivity of siloxycy- clopropane arylation. This cross-coupling proved general to access β-substituted tetralones via ring-expansion of indanone-derived siloxycyclopropanes. The congested, bridging rings of the GB alkaloids were completed using an aluminum-HFIP complex that effected intramolecular cyclization of an acid-labile substrate.</p></div></div></div>

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