Argon-laser-induced fluorescence detection in sodium dodecyl sulfate-capillary gel electrophoretic separations of proteins

Wise, Eric T.; Singh, Navjot; Hogan, Barry L.

doi:10.1016/0021-9673(96)00278-6

Cited by 33 publications

(21 citation statements)

References 27 publications

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“…The suppression of the derivatization reaction by the metal ions could be avoided by the addition of ethylenediaminetetraacetic acid (EDTA) to the reaction medium (Miyano et al, 1985a). The derivatization using NBD-F as a pre-column fluorogenic reagent was applied to the determination of amino acids Imai et al, 1982;Imai, 1983, 1984;Kotaniguchi et al, 1987), amines, amino acids and imino acids , amines and proteins (Miyano et al, 1985b), hexosamines and hexosaminols (Imanari et al, 1985), neutral sugars as their glycamines (Shinomiya et al, 1987), aminophospholipids (Kaneko et al, 1987), Ssulfocysteine and S-sulfoglutathione (Togawa et al, 1988), phosphatidylethanolamine and its lysoform (Saris and Somerharju, 1989), amphetamine-related compounds (Hayakawa et al, 1989), selenium (Nakagawa et al, 1989), cyclamate (Hauck and Köbler, 1990), penicillins (Iwaki et al, 1990), ammonia (Kobayashi et al, 1992), peptides Arg-Gly-NH 2 and Arg-Pro-Lys-Pro (Yoshinaga et al, 1994), cholinergic channel activator A82695 (Hui and Marsh, 1995), dipeptides (Beijersten and Westerlund, 1995), hydrolyzed fumonisin B 1 (Scott and Lawrence, 1996), anatoxin-a (James and Sherlock, 1996;James et al, 1997), proteines (Wise et al, 1996), peptides (Kanazawa et al, 1997) (Jiménez and Mateo, 1997), anatoxin-a, homoanatoxin-a and their degradation products (James et al, 1998), methamphetamine and related compounds , imine-linked opines (Zhang et al, 1998), L-arginine (Prados et al, 1999), D-penicillamine (Al-Majed, 2000) and neurotoxin domic acid (James et al, 2000). Furthermore, after the derivatization with NBD-F, the enantioselective separation of amino acids were achieved on the chiral stationary phases ...…”

Section: Reagentsmentioning

confidence: 99%

Fluorogenic and fluorescent labeling reagents with a benzofurazan skeleton

Uchiyama

Santa

Okiyama

et al. 2001

Biomedical Chromatography

152

101

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Fluorogenic and fluorescent labeling reagents having a benzofurazan (2,1,3-benzoxadiazole) skeleton such as 4-fluoro-7-nitro-2,1,3-benzoxadiazole (NBD-F), 4-N,N-dimethylaminosulfonyl-7-fluoro-2,1,3-benzoxadiazole (DBD-F), 4-aminosulfonyl-7-fluoro-2,1,3-benzoxadiazole (ABD-F), ammonium 7-fluoro-2,1,3-benzoxadiazole-4-sulfonate (SBD-F), 4-hydrazino-7-nitro-2,1,3-benzoxadiazole (NBD-H), 4-N,N-dimethylaminosulfonyl-7-hydrazino-2,1,3-benzoxadiazole (DBD-H), 4-nitro-7-N-piperazino-2,1,3-benzoxadiazole (NBD-PZ), 4-N,N-dimethylaminosulfonyl-7-N-piperazino-2,1,3-benzoxadiazole (DBD-PZ), 4-(N-chloroformylmethyl-N-methyl)amino-7-N,N-dimethylaminosulfonyl-2,1,3-benzoxadiazole (DBD-COCl) and 7-N,N-dimethylaminosulfonyl-4-(2,1,3-benzoxadiazolyl) isothiocyanate (DBD-NCS) are reviewed in terms of synthetic method, reactivity, fluorescence characteristics, sensitivity and application to analytes.

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Section: Reagentsmentioning

confidence: 99%

Fluorogenic and fluorescent labeling reagents with a benzofurazan skeleton

Uchiyama

Santa

Okiyama

et al. 2001

Biomedical Chromatography

152

101

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“…However, NBD-F is of high cost for practical applications compared to 4-chloro-7-nitro-2,1,3-benzoxadiazole (NBD-Cl). Extensive studies have been carried out in applying NBD-Cl derivatization to the detection of biogenic amines such as amino acids [17] and proteins [18]. Uchiyama et al [19] have made an in-depth review on this topic.…”

Section: Introductionmentioning

confidence: 99%

Simultaneous determination of catecholamines and amino acids by micellar electrokinetic chromatography with laser‐induced fluorescence detection

Zhou

Wang

Tian

et al. 2007

J of Separation Science

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A selective and sensitive method was developed for separation and simultaneous determination of catecholamines and amino acids by MEKC with LIF. Interestingly enough, such work has been firstly performed on catecholamines derivatized with 4-chloro-7-nitro-2,1,3-benzoxadiazole and the detailed derivatization mechanism was discussed. After derivatization at 60 degrees C for 20 min, NBD-labeled catecholamines and amino acids were separated in a buffer system containing 10 mM sodium tetraborate-Na2HPO4, 20 mM SDS, and 10% v/v ACN at pH 9.75. SDS micelles were employed to improve the fluorescence intensity of catecholamine derivatives efficiently. Under optimum conditions, two catecholamines and 11 amino acids were separated in a short 13 min analysis time and the RSDs for migration time and peak area were less than 0.60 and 6.50%, respectively. The method was successfully applied for the quantification of catecholamines and amino acids in Portulaca oleracea L., human urine sample, and mixed injection sample.

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“…When more sensitive methods than UV detection are required, laser-induced fluorescence (LIF) or mass spectrometry methods have been used. The detection limit for bovine serum albumin (BSA) decreases from 0.5 ~lg mL -1 to 25 ng mL -1 when UV absorption is replaced with argon-laser-induced fluorescence [19]. In his subsequent review, Dolnik [7] updated the information on these same topics.…”

Section: Czementioning

confidence: 98%

Capillary Electrophoresis in the Development of Recombinant Protein Biopharmaceuticals

Chen¹,

Canova-Davis²

2001

CE in Biotechnology: Practical Applications for Protein and Peptide Analyses

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The understanding of the physicochemical properties of proteins in solution is required to understand the separations taking place in the capillary. For example, during isoelectric focusing, it is important to ensure the lack of protein precipitation during fOCUSing and mobilization otherwise artifacts occur and the true resolution of charge variants is not achieved. Similarly, buffer conditions, including additives, composition of buffer, and pH can influence the resolution of product variants. With diligent efforts one can achieve desired separations. As knowledge of buffer conditions and use of these techniques increase, the methods will be improved.MECC can be useful for the characterization of recombinant proteins and monoclonal antibodies. However, the relatively long analyte migration times may be a deterrent for routine use in quality control situations. Pharmaceutical companies will employ new techniques which provide advantages over current technology. CE has advantages in certain applications. Applications which use slab gel techniques, IEF and SDS-PAGE can be replaced by the CE methods for formulation development, characterization of charge isoforms, and for purity determinations. CZE and clEF can be used for rapid identity tests which do not require peptide mapping. CZE has a tremendous advantage in analyzing basic proteins, and CZE and CE-SDS can be used to quantify product in the presence of interfering excipients. It is the responsibility of the analytical chemist to determine applications which are appropriate for CEo It is apparent that these are currently being defined for the biotechnology industry, and the usage of CE should continue to increase.

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Argon-laser-induced fluorescence detection in sodium dodecyl sulfate-capillary gel electrophoretic separations of proteins

Cited by 33 publications

References 27 publications

Fluorogenic and fluorescent labeling reagents with a benzofurazan skeleton

Fluorogenic and fluorescent labeling reagents with a benzofurazan skeleton

Simultaneous determination of catecholamines and amino acids by micellar electrokinetic chromatography with laser‐induced fluorescence detection

Capillary Electrophoresis in the Development of Recombinant Protein Biopharmaceuticals

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