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Camptothecin, an anticancer component from Camptotheca acuminate, mayinteract with human serum albumin (HSA) at the subdomain IIA (site I), and then convert toits inactive form(carboxylate form). In this paper, the detailed electrochemical behaviors ofcamptothecin at a pyrolytic graphite electrode is presented. The interaction betweencamptothecin and HSA is also studied by electrochemical technique. By comparing withbovine serum albumin (BSA), which is highly homologous to HSA, we prove thatcamptothecin can specifically bind to HSA. Meanwhile, the inhibitory influence of sodiumsalicylate to this binding is also discussed.