Reversed-Phase HPLC: Preparation and Characterization of Reversed-Phase Stationary Phases

1998 ◽  
pp. 311-342
Keyword(s):  
Stationary Phases ◽  
Reversed Phase ◽  
Reversed Phase Hplc

Immobilized Polysaccharide-Based Stationary Phases for Enantioseparation in Normal Versus Reversed Phase HPLC

2014 ◽  
Vol 78 (13-14) ◽  
pp. 909-915 ◽  
Author(s):  
Radim Geryk ◽  
Květa Kalíková ◽  
Jiří Vozka ◽  
Eva Tesařová
Keyword(s):  
Stationary Phases ◽  
Reversed Phase ◽  
Reversed Phase Hplc

Characterization of in vitro proteolytic processing of β-endorphin by reversed-phase HPLC

Peptides ◽  
1984 ◽  
Vol 5 (6) ◽  
pp. 1037-1042 ◽  
Author(s):  
Thomas P. Davis ◽  
Hans Schoemaker ◽  
Alison J. Culling-Berglund
Keyword(s):  
Reversed Phase ◽  
Proteolytic Processing ◽  
Reversed Phase Hplc

Chiral Chromatography Studies of Chemical Behavior of Cinacalcet on Polysaccharide Chiral Reversed-Phase HPLC Stationary Phases

2012 ◽  
Vol 95 (6) ◽  
pp. 1639-1643 ◽  
Author(s):  
Michal Douša ◽  
Jiřiacute; Břicháč
Keyword(s):  
Chiral Stationary Phase ◽  
Stationary Phases ◽  
Active Pharmaceutical Ingredient ◽  
Reversed Phase ◽  
Hplc Method ◽  
Reversed Phase Hplc ◽  
Chiral Chromatography ◽  
Chemical Behavior ◽  
Analytical Resolution

Abstract A rapid HPLC method for the analytical resolution of cinacalcet enantiomers was developed. Four chiral columns (two amylose and two cellulose type) were evaluated in RP systems. Excellent enantioseparation with a resolution of more than 6 was achieved on Chiralpak AY (amylose 5-chloro-2-methylphenylcarbamate chiral stationary phase) using 10 mM triethylamine (pH 8.0)–acetonitrile (40 + 60, v/v) mobile phase. Validation of the HPLC method, including linearity, LOD, LOQ, precision, accuracy, and selectivity, was performed according to the International Conference on Harmonization guidelines. The method was successfully applied for the determination of (S)-cinacalcet in enantiopure active pharmaceutical ingredient (R)-cinacalcet.

scholarly journals Purification and characterization of an L-glutamic acid60-L-alanine30-L-tyrosine10 (GAT)-specific suppressor factor from genetic responder mice.

1983 ◽  
Vol 158 (4) ◽  
pp. 1034-1047 ◽  
Author(s):  
C M Sorensen ◽  
C W Pierce ◽  
D R Webb
Keyword(s):  
Specific Activity ◽  
Reversed Phase ◽  
Biologically Active ◽  
Reversed Phase Hplc ◽  
Purification And Characterization ◽  
Suppressor Factor ◽  
Chemical Homogeneity ◽  
T Cell Factor ◽  
Molecular Weights

A hybridoma-derived, GAT-specific suppressor T cell factor (GAT-TsFR) from responder C57BL/10 mice has been purified to apparent chemical homogeneity using reversed phase HPLC techniques. 40 l of starting material yielded approximately 880 micrograms protein with a specific activity of 28.4 X 10(3) S50 U/ng protein representing a purification factor of 4.2 X 10(6). Purified GAT-TsFR is a hydrophobic protein with a minimum molecular weight of 18,000 that is capable of forming biologically active aggregates with molecular weights of 28,000, 64,000 and approximately 84,000 and has a pI of 6.4. GAT-TsFR is a glycoprotein that binds GAT and GT, but not GA, and bears determinants encoded by the I-J subregion of the H-2 complex. This GAT-TsFR derived from an H-2b responder haplotype to GAT is compared with GAT-TsF derived from the nonresponder H-2q haplotype on the basis of biochemical and some serological properties.

Sign in / Sign up

Export Citation Format

Share Document