Ferromagnetism in a Mixture of Antiferromagnetic FeTiO3 and -Fe2O3 as Observed by Using M?ssbauer Spectroscopy

Kim, Woochul; Park, Il Jin; Kim, Chul Sung

doi:10.3938/jkps.53.1529

Cited by 1 publication

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A number of methods, such as surface plasmon resonance (SPR) [1][2][3][4][5][6][7], enzyme-linked immunosorbent assay (ELISA) [8][9][10][11][12][13][14][15][16], FRET-based homogenous immunoassay [17][18][19], isothermal calorimetry (ITC) [20][21][22][23], high performance size exclusion chromatography (HPSEC) [24][25][26], microarray [27][28][29][30][31] and many others, have been tried for antibodyantigen interactions. Although there were several successful applications, some accurate online chromatographic analysis for fast antibody-antigen interaction is still in need to improve our understanding of the antibody-antigen interaction.…”

Section: Introductionmentioning

confidence: 99%

In‐capillary detection of fast antibody‐peptide binding using fluorescence coupled capillary electrophoresis

et al. 2015

View full text Add to dashboard Cite

Herein, we report a technique for detecting the fast binding of antibody-peptide inside a capillary. Anti-HA was mixed and interacted with FAM-labeled HA tag (FAM-E4 ) inside the capillary. Fluorescence coupled capillary electrophoresis (CE-FL) was employed to measure and record the binding process. The efficiency of the antibody-peptide binding on in-capillary assays was found to be affected by the molar ratio. Furthermore, the stability of anti-HA-FAM-E4 complex was investigated as well. The results indicated that E4 YPYDVPDYA (E4) or TAMRA-E4 YPYDVPDYA (TAMRA-E4) had the same binding priorities with anti-HA. The addition of excess E4 or TAMRA-E4 could lead to partial dissociation of the complex and take a two-step mechanism including dissociation and association. This method can be applied to detect a wide range of biomolecular interactions.

show abstract