Human serum albumin (HSA), as one of the most abundant carrier protein, is generally considered to play a crucial role in the transportation and disposition of numerous endogenous and exogenous compounds [1]. The interaction of new salen-co(III) of N,N΄- dipyridoxyl (1,4-butanediamine) Schiff-base complex with DNA using melting temperature, fluorescence spectrometry and gel electrophoresis techniques has been studied by Z. Mashhadi Khoshkhoo et al. [2]. Cytotoxicity effects Cobalt-salen, which is synthesized by salicylaldehyde interaction was compared with two common anticancer drugs, cisplatin and vincristine, has been investigated by S. Mollazade et al. [3]. The objective of this work is to study the interaction of the cobalt (III)-salenwith human serum albumin (HSA) in physiological buffer solution (pH = 7.4) making use of UV spectroscopy.The binding parameters evaluated by spectroscopy method [4]. The microscopic binding constant (k), binding capacity (g) and Hill constant (nH) have been estimated to be 3.854×104 M-1, 3, and 0.904, respectively, according to Hill equation. The results revealed that the Hill constant is less than 1 (nH< 1) which indicated that the system has negative cooperative in binding process; and this result coincided with Scatchard plot.

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