THE PREPARATION OF D-RIBOSE-1-C14, D-ARABINOSE-1-C14, AND D-2-DEOXYRIBOSE-1-C14

1959 ◽  
Vol 37 (10) ◽  
pp. 1776-1781 ◽  
Author(s):  
D. H. Murray ◽  
G. C. Butler

D-Ribose-1-C14 and D-arabinose-1-C14 have been synthesized by a modified Sowden–Fischer procedure in which the mixed sodium nitropentitols resulting from the condensation of erythrose and C14H3NO2 have been submitted to a Nef reaction. The epimeric labelled pentoses were isolated by cellulose column chromatography in an over-all radiochemical yield of 19%.Mixed nitropentitols-1-C14 have been acetylated, partially deacetylated with sodium bicarbonate in a non-polar solvent, and hydrogenated to yield triacetoxy-1-nitropentane-1-C14. The mixture of this material and the accompanying undeacetylated nitropentitols gave rise, via a Nef reaction, to D-2-deoxyribose-1-C14 (6.3%), D-ribose-1-C14 (3.1%), and D-arabinose-1-C14 (2.9%).

1977 ◽  
Vol 74 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Y.S. Shin-Buehring ◽  
M. Osang ◽  
R. Ziegler ◽  
J. Schaub

2009 ◽  
Vol 56 (1) ◽  
pp. 13-16
Author(s):  
Ken Sakai ◽  
Kyohei Ohtaki ◽  
Hideyo Koizumi ◽  
Shota Sato ◽  
Hisaoki Suzuki ◽  
...  

1990 ◽  
Vol 269 (1) ◽  
pp. 13-18 ◽  
Author(s):  
Y Homma ◽  
Y Emori ◽  
F Shibasaki ◽  
K Suzuki ◽  
T Takenawa

A novel bovine spleen phosphoinositide-specific phospholipase C (PLC) has been identified with respect to immunoreactivity with four independent antibodies against each of the PLC isoenzymes, and purified to near homogeneity by sequential column chromatography. Spleen contains three of the isoenzymes: two different gamma-types [gamma 1 and gamma 2, originally named as PLC-gamma [Rhee, Suh, Ryu & Lee (1989) Science 244, 546-550] and PLC-IV [Emori, Homma, Sorimachi, Kawasaki, Nakanishi, Suzuki & Takenawa (1989) J. Biol. Chem. 264, 21885-21890] respectively] and delta-type of the enzyme, but PLC-gamma 1 is separated from the PLC-gamma 2 pool by the first DEAE-cellulose column chromatography. Subsequently, PLC-delta is dissociated on the third heparin-Sepharose column chromatography. The purified enzyme has a molecular mass of 145 kDa on SDS/polyacrylamide-gel electrophoresis and a specific activity of 12.8 mumol/min per mg with phosphatidylinositol 4,5-bisphosphate as substrate. This enzyme activity is dependent on Ca2+ for hydrolysis of all these phosphoinositides. None of the other phospholipids examined could be its substrate at any concentration of Ca2+. The optimal pH of the enzyme is slightly acidic (pH 5.0-6.5).


1976 ◽  
Vol 22 (7) ◽  
pp. 1047-1052 ◽  
Author(s):  
A Zettner ◽  
P E Duly

Abstract On diethylaminoethyl-cellulose column chromatography, the folate binding protein in the serum of 21 patients eluted in the early effluents as a single sharply defined peak. The chromatographic behavior of the folate binder remained unchanged whether or not the serum was, before chromatography, complexed with tritium-labeled pteroylglutamic acid ([3H]PGA), dialyzed, or charcoal-adsorbed. Heating to 100 degrees C for 10 min dissociated the [3H]PGA-binder complex while destroying the folate binding property. The presence or appearance of this folate binder in increased amounts in the serum of patients with various diseases may be related to conditions of increased tissue turnover.


1958 ◽  
Vol 75 (1) ◽  
pp. 56-68 ◽  
Author(s):  
A. Angapindu ◽  
H. Silberman ◽  
P. Tantivatana ◽  
I.R. Kaplan

Nature ◽  
1962 ◽  
Vol 193 (4817) ◽  
pp. 801-802 ◽  
Author(s):  
E. D. GARBER ◽  
W. F. REDDING ◽  
W. CHORNEY

1983 ◽  
Vol 213 (1) ◽  
pp. 39-41 ◽  
Author(s):  
M L Guinea ◽  
N Tamiya ◽  
H G Cogger

Erabutoxins a and b, the major neurotoxins in the venom of the sea snake Laticauda semifasciata, were detected in the venom of Laticauda schistorhynchus. The identity of the toxins was confirmed on the basis of elution position on CM-cellulose column chromatography, disc electrophoretic mobility, amino acid analysis and toxicity measurement.


Sign in / Sign up

Export Citation Format

Share Document