Tissue factor (TF, tissue thromboplastin) is a membrane bound glycoprotein, which acceler-ates the blood clotting, activating both the intrinsic and the extrinsic pathways to serve as a cofactor for activated factor VII (Vila). The TF-factor Vila complex (TF/VIIa) proteolytically activates factors IX and X, which leads to the generation of thrombin and fibrin clots. In order to isolate TF inhibitors, by means of a bioassay-directed chromatographic separation technique, from the leaves of Eriobotrya japonica Lindley (Rosaceae), a known sesquiterpene glycoside (2) and ferulic acid (3) were isolated as inhibitors that were evaluated using a single-clotting assay method for determining TF activity. Another sesquiterpene glycoside (1) was also isolated but was inactive in the assay system. Compound 3 was yielded by alkaline hydrolysis of compound 2. The structures of compounds 1, 2, and 3 were identified by means of spectral analysis as $3-O-{alph}-L-rhamnopyranosyl-(1{ ightarrow}4)-a-L-rhamnopyranosyl-(1{ ightarrow}2)-[{alph}-L-rhamnopyrano-syl-(1{ ightarrow}6)]-{eta}-D-glucopyranosyl nerolidol$ (1), $3-O-{alph}-L-rhamnopyranosyl-(1{ ightarrow}4)-{alph}-L-rhamnopyr-anosyl-(1{ ightarrow}2)-[{alph}-L-(4-trans-feruloyl)-rhamnopyranosyl-(1{ ightarrow}6)]-{eta}-D-glucopyranosyl$ nerolidol (2) and ferulic acid (3), respectively. Compounds 2 and 3 inhibited 50% of the TF activity at con-centrations of 2 and $369{;}mu extrm{m}/TF$ units, respectively.