scholarly journals Process for the Purification of cis-p-Coumaric Acid by Cellulose Column Chromatography after the Treatment of the trans Isomer with Ultraviolet Irradiation

2018 ◽  
Vol 34 (10) ◽  
pp. 1195-1199 ◽  
Author(s):  
Takahiko MITANI ◽  
Hisa MIMURA ◽  
Keiko IKEDA ◽  
Mitsunori NISHIDE ◽  
Masanori YAMAGUCHI ◽  
...  
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