کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1235403 | 1495269 | 2012 | 6 صفحه PDF | دانلود رایگان |

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.
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► 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.
Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 99, 15 December 2012, Pages 373–378