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Comparison of the “zero crossing” method in derivative spectroscopy and ultrafiltration for the determination of free and bound fractions of mitoxantrone
Author(s) -
Maia MBS,
Tufenkji AE,
Rochas MA,
Saivin S.,
Houin G.
Publication year - 1994
Publication title -
fundamental and clinical pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.655
H-Index - 73
eISSN - 1472-8206
pISSN - 0767-3981
DOI - 10.1111/j.1472-8206.1994.tb00795.x
Subject(s) - mitoxantrone , ultrafiltration (renal) , derivative (finance) , zero crossing , zero (linguistics) , chemistry , chromatography , spectroscopy , analytical chemistry (journal) , medicine , physics , thermodynamics , philosophy , chemotherapy , financial economics , economics , power (physics) , linguistics , quantum mechanics
Summary— In vitro mitoxantrone binding to human serum, human serum albumin (HSA, 600 μM) and alpha‐1‐acid glycoprotein (AAG, 15 μM) was investigated by ultrafiltration and the first‐derivative spectrophotometry based on the “zero crossing” method. The binding of mitoxantrone to isolated proteins was studied at eight concentrations whose range depended on the protein used. The results showed that mitoxantrone binding to human plasma and HSA involved a saturable binding. The AAG binding involved a saturable binding followed by a non saturable process. Within the concentration range studied, the percent and binding parameters which characterize the drug‐protein interaction were comparable in both methods.