Melinda Andrási
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Melinda Andrási has a total of 13 co-authors. Here are the top co-authors by number of shared publications:
Attila Gáspár
University of Debrecen
2 shared publicationsAndrás Pungor
Department of Experimental Physics, University of Debrecen, Debrecen, Hungary
1 shared publication- Attila Gáspár
Department of Chemistry and Biochemistry, California State University, Los Angeles, CA 90032-8202, USA
1 shared publication Balint Zagyi
Department of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen, Hungary
1 shared publication- Cynthia Nagy
Department of Inorganic and Analytical Chemistry, University of Debrecen, Egyetem tér 1., H-4032 Debrecen, Hungary
1 shared publication Gyöngyi Gyémánt
Department of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen, Hungary
1 shared publication
Latest Publications
- Open Access
- 6 September 2023
- Published by Springer Nature in Chromatographia
- Vol. 86 (10) , 659-668
Study of Effect of Incubation Time and Temperature on the Linear Polyacrylamide-Coating Performance for the Separation of Proteins by Capillary Zone Electrophoresis
The preparation of linear polyacrylamide (LPA)-coated capillary is a multistep, laborious process. In this study, five different LPA-coating procedures were compared regarding the capillary pretreatment (incubation time and temperature), the formation of the intermediate silyl layer and the attachment of the polymer top layer. LPA coatings were examined by the analysis of a standard mixture solution of insulin, rituximab and hemoglobin using a background electrolyte (BGE) of 50 mM HCOOH (pH 2.6). The results were contrasted with those that were obtained using the bare fused-silica capillary. The reproducibility of the simplest LPA-coating preparation was tested. The long-term stability of the capillary coating was evaluated through inter-day precision data using a large number of injections of the three-protein test mixture solution. The implementation of a short-term procedure at elevated temperature, guided by a comprehensive review of various conditions documented in the literature, yielded an efficiently functional LPA coating.
- 6 September 2023
- Published by Springer Nature in Chromatographia
- Vol. 86 (10) , 659-668
Open AccessStudy of Effect of Incubation Time and Temperature on the Linear Polyacrylamide-Coating Performance for the Separation of Proteins by Capillary Zone Electrophoresis
The preparation of linear polyacrylamide (LPA)-coated capillary is a multistep, laborious process. In this study, five different LPA-coating procedures were compared regarding the capillary pretreatment (incubation time and temperature), the formation of the intermediate silyl layer and the attachment of the polymer top layer. LPA coatings were examined by the analysis of a standard mixture solution of insulin, rituximab and hemoglobin using a background electrolyte (BGE) of 50 mM HCOOH (pH 2.6). The results were contrasted with those that were obtained using the bare fused-silica capillary. The reproducibility of the simplest LPA-coating preparation was tested. The long-term stability of the capillary coating was evaluated through inter-day precision data using a large number of injections of the three-protein test mixture solution. The implementation of a short-term procedure at elevated temperature, guided by a comprehensive review of various conditions documented in the literature, yielded an efficiently functional LPA coating.
- Open Access
- 23 February 2023
- Published by MDPI AG in Separations
- Vol. 10 (3) , 150
Analysis of Sugars in Honey Samples by Capillary Zone Electrophoresis Using Fluorescence Detection
The applicability of capillary electrophoresis (CE) with light-emitting diode-induced fluorescence detection (LEDIF) for the separation of sugars in honey samples was studied. An amount of 25 mM ammonium acetate (pH 4.5) with 0.3% polyethylene oxide (PEO) was found to be optimal for the efficient separation of carbohydrates. 8-aminopyrene-1,3,6-trisulfonic acid (APTS) was used for the labeling of the carbohydrate standards and honey sugars for fluorescence detection. The optimized method was applied in the quantitative analysis of fructose and glucose by direct injection of honey samples. Apart from the labeling reaction, no other sample preparation was performed. The mean values of the fructose/glucose ratio for phacelia honey, acacia honey and honeydew honey were 0.86, 1.61 and 1.42, respectively. The proposed method provides high separation efficiency and sensitive detection within a short analysis time. Apart from the labeling reaction, it enables the injection of honeys without sample pretreatment. This is the first time that fluorescence detection has been applied for the CE analysis of sugars in honeys.
- 23 February 2023
- Published by MDPI AG in Separations
- Vol. 10 (3) , 150
Open AccessAnalysis of Sugars in Honey Samples by Capillary Zone Electrophoresis Using Fluorescence Detection
The applicability of capillary electrophoresis (CE) with light-emitting diode-induced fluorescence detection (LEDIF) for the separation of sugars in honey samples was studied. An amount of 25 mM ammonium acetate (pH 4.5) with 0.3% polyethylene oxide (PEO) was found to be optimal for the efficient separation of carbohydrates. 8-aminopyrene-1,3,6-trisulfonic acid (APTS) was used for the labeling of the carbohydrate standards and honey sugars for fluorescence detection. The optimized method was applied in the quantitative analysis of fructose and glucose by direct injection of honey samples. Apart from the labeling reaction, no other sample preparation was performed. The mean values of the fructose/glucose ratio for phacelia honey, acacia honey and honeydew honey were 0.86, 1.61 and 1.42, respectively. The proposed method provides high separation efficiency and sensitive detection within a short analysis time. Apart from the labeling reaction, it enables the injection of honeys without sample pretreatment. This is the first time that fluorescence detection has been applied for the CE analysis of sugars in honeys.
- 23 October 2015
- Published by Pleiades Publishing Ltd in Journal of Analytical Chemistry
- Vol. 70 (11) , 1360-1367
Study on repeatability of the determination of temozolomide by micellar electrokinetic capillary chromatography using internal standards
This paper demonstrates the study of the use of single or multiple (2–4) internal standards for the improvement of the repeatability of the micellar electrokinetic capillary chromatographic measuremen
- 23 October 2015
- Published by Pleiades Publishing Ltd in Journal of Analytical Chemistry
- Vol. 70 (11) , 1360-1367
Study on repeatability of the determination of temozolomide by micellar electrokinetic capillary chromatography using internal standards
This paper demonstrates the study of the use of single or multiple (2–4) internal standards for the improvement of the repeatability of the micellar electrokinetic capillary chromatographic measuremen
- 17 December 2014
- Published by Wiley in Electrophoresis
- Vol. 36 (11-12) , 1274-1281
A comparative study of capillary electrophoresis and isothermal titration calorimetry for the determination of binding constant of human serum albumin to monoclonal antibody
This paper focuses on the investigation of the interactions between the anti‐HSA‐mAb and its protein antigen using CZE, ACE, and isothermal titration calorimetry. The CZE revealed the formation of the anti‐HSA‐mAb·HSA and anti‐HSA‐mAb·(HSA)2 complexes and the binding constants determined by plotting the amount of the bound anti‐HSA‐mAb as a function of the concentration of HSA. The ACE provided information on the binding strength from the change in effective electrophoretic mobility of the anti‐HSA‐mAb. These two separation techniques estimated the presence of two binding sites. The equilibrium dissociation constant values obtained by CZE and ACE were found to be 2.26 × 10−6 M for anti‐HSA‐mAb·HSA, 1.22 × 10−6 M for anti‐HSA‐mAb·(HSA)2 and 4.45 × 10−8 M for anti‐HSA‐mAb·HSA, 1.08 × 10−7 M for anti‐HSA‐mAb·(HSA)2, respectively. The dissociation constant data obtained by ACE were in congruence with the values obtained by isothermal titration calorimetry (2.74 × 10−8 M, 1.04 × 10−7 M).
- 17 December 2014
- Published by Wiley in Electrophoresis
- Vol. 36 (11-12) , 1274-1281
A comparative study of capillary electrophoresis and isothermal titration calorimetry for the determination of binding constant of human serum albumin to monoclonal antibody
This paper focuses on the investigation of the interactions between the anti‐HSA‐mAb and its protein antigen using CZE, ACE, and isothermal titration calorimetry. The CZE revealed the formation of the anti‐HSA‐mAb·HSA and anti‐HSA‐mAb·(HSA)2 complexes and the binding constants determined by plotting the amount of the bound anti‐HSA‐mAb as a function of the concentration of HSA. The ACE provided information on the binding strength from the change in effective electrophoretic mobility of the anti‐HSA‐mAb. These two separation techniques estimated the presence of two binding sites. The equilibrium dissociation constant values obtained by CZE and ACE were found to be 2.26 × 10−6 M for anti‐HSA‐mAb·HSA, 1.22 × 10−6 M for anti‐HSA‐mAb·(HSA)2 and 4.45 × 10−8 M for anti‐HSA‐mAb·HSA, 1.08 × 10−7 M for anti‐HSA‐mAb·(HSA)2, respectively. The dissociation constant data obtained by ACE were in congruence with the values obtained by isothermal titration calorimetry (2.74 × 10−8 M, 1.04 × 10−7 M).
- 1 February 2007
- Published by Elsevier in Journal of Chromatography B
- Vol. 846 (1-2) , 355-358
Analysis of cephalosporins in bronchial secretions by capillary electrophoresis after simple pretreatment
- 1 February 2007
- Published by Elsevier in Journal of Chromatography B
- Vol. 846 (1-2) , 355-358
Analysis of cephalosporins in bronchial secretions by capillary electrophoresis after simple pretreatment