| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1235403 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2012 | 6 Pages |
It is found that the fluorescence intensity of Morin can be strongly quenched by proteins. Based on this, a new fluorimetric method for the determination of protein was developed. Under optimum conditions, the quenchment of Morin fluorescence was in proportion to the concentration of proteins in the range 0.0001–0.1000 g · L−1 for bovine serum albumin (BSA) and 0.0005–0.1000 g · L−1 for human serum albumin (HSA). The reaction mechanism indicates that proteins can bind with Morin at the 3-hydroxyl and the 4-carbonyl and form a non-fluorescence complex 4:1 molar ratio of Morin/BSA, which results in the fluorescence of Morin and BSA are all quenched.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Morin can combine with BSA form a non-fluorescence complex 4:1 molar ratio of Morin/BSA. ► Morin can bind with proteins at its 3-hydroxyl and the 4-carbonyl. ► A new fluorescence method for determination of proteins is established.
