1. The interaction of cationic and anionic porphyrins with the bovine serum albumin in borate buffer
- Author
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Yury A. Gubarev, Oskar I. Koifman, and Natalya Sh. Lebedeva
- Subjects
Chromatography ,biology ,010405 organic chemistry ,Chemistry ,Albumin ,Cationic polymerization ,General Chemistry ,010402 general chemistry ,Condensed Matter Physics ,01 natural sciences ,Fluorescence spectroscopy ,0104 chemical sciences ,BORATE BUFFER ,polycyclic compounds ,Native state ,biology.protein ,heterocyclic compounds ,Bovine serum albumin ,Food Science - Abstract
The interaction of water-soluble porphyrins with the bovine serum albumin in borate buffer at pH 8.6 has been studied. The localization of porphyrins in the protein globule has been determined. It was established that the native conformation of albumin upon binding with the porphyrins is preserved, however, the anionic porphyrins are exhibit wedging effect on the albumin domains. The binding constants were obtained from fluorescence spectroscopy data.
- Published
- 2017
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