scholarly journals Ion Exchange Chromatography and Mass Spectrometric Methods for Analysis of Cadmium-Phytochelatin (II) Complexes

2013 ◽  
Vol 10 (4) ◽  
pp. 1304-1311 ◽  
Author(s):  
Miguel Rodrigo ◽  
Natalia Cernei ◽  
Marketa Kominkova ◽  
Ondrej Zitka ◽  
Miroslava Beklova ◽  
...  
1975 ◽  
Vol 53 (1) ◽  
pp. 65-69 ◽  
Author(s):  
S. R. Philips ◽  
B. A. Davis ◽  
D. A. Durden ◽  
Alan A. Boulton

A procedure for the quantitative evaluation of m-tyramine in mammalian tissues is described. It involves isolation of the amine by ion-exchange chromatography, followed by conversion to the dansyl derivative, chromatographic separation, and quantitation by the mass spectrometric integrated ion current technique using an isotopically labelled internal standard. The concentrations of m-tyramine in some tissues of male Wistar rats were (mean ± S.D., nanograms per gram): brain 0.32 ± 0.03, heart 0.44 ± 0.13. kidney 12.6 ± 3.4, liver 0.27 ± 0.04, lung 0.33 ± 0.11, spleen 0.25 ± 0.07, and blood 0.15 ± 0.04.


2021 ◽  
Vol 8 ◽  
Author(s):  
Jaber A. Alshehri ◽  
Daniel M. Gill ◽  
Alan M. Jones

The treatment of common steroids: estrone, estradiol, cortisol, and pregnenolone with tributylsulfoammonium betaine (TBSAB) provides a convenient chemoselective conversion of the steroids alcohol/phenol moiety to the corresponding steroidal organosulfate. An important feature of the disclosed methodology is the millimolar scale of the reaction, and the isolation of the corresponding steroid sulfates as their biologically relevant sodium salts without the need for ion-exchange chromatography. The scope of the method was further explored in the estradiol and pregnanediol steroid systems with the bis-sulfated derivatives. Ultimately, a method to install an isotopic label, deuterium (2H) combined with estrone sulfation is a valuable tool for its mass-spectrometric quantification in biological studies.


1974 ◽  
Vol 52 (5) ◽  
pp. 366-373 ◽  
Author(s):  
S. R. Philips ◽  
D. A. Durden ◽  
A. A. Boulton

A procedure for the quantitative evaluation of p-tyramine in mammalian tissues is described. It involves isolation of the amine by ion-exchange chromatography, followed by conversion to the dansyl derivative, chromatographic separation, and quantitation by the mass spectrometric integrated ion current technique using an isotopically labelled internal standard.The concentrations of p-tyramine in some tissues of male Wistar rats were (mean ± standard deviation (ng/g)): brain 2.0 ± 0.9, heart 3.4 ± 1.4, kidney 32.7 ± 13.1, liver 1.5 ± 0.5, lung 3.0 ± 1.2, and spleen 3.4 ± 1.2. In the brain, hypothalamus contained 11.3 ± 3.7, cerebellum 2.3 ± 1.7, stem 2.2 ± 1.0, caudate nucleus 19.2 ± 2.5, and the 'rest' 1.6 ± 0.4 ng/g, respectively.


1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.


2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa

Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.


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