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The interaction of serpentine and seroalbumin by fluorescence quenching

Queraltó, A.; Hidalgo, J.; Sánchez, M.

Il Farmaco; Edizione Pratica 41(10): 338-346

1986

ISSN/ISBN: 0430-0912
PMID: 3792536
Document Number: 269472
The study of fluorescence quenching of human serum albumin (H.S.A.) and bovine serum albumin (B.S.A.) by serpentine allows the deduction of the average constant of complex formation, and the values of the thermodynamic parameters .DELTA.Go, .DELTA.Ho, and .DELTA.So, at various temperatures and molarities of S.A. An explanation of the binding process is proposed, which involves hydrogen bonding electrostatic interactions, and hydrophobic bonds.

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