Optical Resolution of Some Alkaloids by Paper Chromatography and Cellulose Column Chromatography

ABSTRACT Perfusion of rat liver with vanillic acid yielded only one metabolite. In paper chromatography with three different solvent systems, the substance showed the same RF-values as vanillyolglycine (3-methoxy-4-hydroxyhippuric acid) and in mixed chromatograms there was only one single spot. After separation by column chromatography, the UV- and IRspectra of the reaction product were identical with those of 3-methoxy4-hydroxy-hippuric acid. During the perfusion experiment, the kinetics of the conjugation were investigated.

Download Full-text

Clay column chromatography for optical resolution: selectivities of Λ-[Ru(phen)3]2+ and Λ-[Ru(bpy)3]2+ laponite columns towards 1,1′-binaphthol

Applied Clay Science ◽

10.1016/0169-1317(96)00010-5 ◽

1996 ◽

Vol 11 (1) ◽

pp. 1-10 ◽

Cited By ~ 23

Author(s):

Akihiko Yamagishi ◽

Masahiro Taniguchi ◽

Yoshimi Imamura ◽

Hisako Sato

Keyword(s):

Column Chromatography ◽

Optical Resolution

Download Full-text

A simple assay for galactokinase using deae-cellulose column chromatography

Clinica Chimica Acta ◽

10.1016/0009-8981(77)90379-5 ◽

1977 ◽

Vol 74 (1) ◽

pp. 1-5 ◽

Cited By ~ 21

Author(s):

Y.S. Shin-Buehring ◽

M. Osang ◽

R. Ziegler ◽

J. Schaub

Keyword(s):

Column Chromatography ◽

Deae Cellulose ◽

Deae Cellulose Column ◽

Cellulose Column

Download Full-text

THE OPTICAL RESOLUTION OF DL-AMINO ACID MENTHYL ESTER DERIVATIVES BY PAPER CHROMATOGRAPHY

Chemistry Letters ◽

10.1246/cl.1972.269 ◽

1972 ◽

Vol 1 (4) ◽

pp. 269-272

Author(s):

Isamu Akiyama ◽

Masaji Onaya ◽

Akira Hayakawa ◽

Yojiro Tsuzuki

Keyword(s):

Amino Acid ◽

Paper Chromatography ◽

Optical Resolution

Download Full-text

Effective Purification of 1,4-.BETA.-Endoglucanase (EG66) from a Marine Mollusc, Patinopecten yessoensis, by Cellulose Column Chromatography

Journal of Applied Glycoscience ◽

10.5458/jag.56.13 ◽

2009 ◽

Vol 56 (1) ◽

pp. 13-16

Author(s):

Ken Sakai ◽

Kyohei Ohtaki ◽

Hideyo Koizumi ◽

Shota Sato ◽

Hisaoki Suzuki ◽

...

Keyword(s):

Column Chromatography ◽

Patinopecten Yessoensis ◽

Marine Mollusc ◽

Cellulose Column

Download Full-text

Isolation and characterization of a γ-type phosphoinositide-specific phospholipase C (PLC-γ2)

Biochemical Journal ◽

10.1042/bj2690013 ◽

1990 ◽

Vol 269 (1) ◽

pp. 13-18 ◽

Cited By ~ 39

Author(s):

Y Homma ◽

Y Emori ◽

F Shibasaki ◽

K Suzuki ◽

T Takenawa

Keyword(s):

Phospholipase C ◽

Column Chromatography ◽

Specific Activity ◽

Polyacrylamide Gel Electrophoresis ◽

Deae Cellulose ◽

Isolation And Characterization ◽

Delta Type ◽

Hydrolysis Of ◽

Cellulose Column

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).

Download Full-text

Separation of folate binding protein from human serum by DEAE-cellulose column chromatography.

Clinical Chemistry ◽

10.1093/clinchem/22.7.1047 ◽

1976 ◽

Vol 22 (7) ◽

pp. 1047-1052 ◽

Cited By ~ 3

Author(s):

A Zettner ◽

P E Duly

Keyword(s):

Human Serum ◽

Column Chromatography ◽

Binding Protein ◽

Deae Cellulose ◽

Chromatographic Behavior ◽

Binding Property ◽

Folate Binding Protein ◽

Diethylaminoethyl Cellulose ◽

Pteroylglutamic Acid ◽

Cellulose Column

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.

Download Full-text