Cratoxylum cochinchinense displayed significant inhibition against protein tyrosine phosphatase 1B (PTP1B) and α-glucosidase, both of which are key target enzymes to attenuate diabetes and obesity. The compounds responsible for both enzymes inhibition were identified as twelve xanthones (1–12) among which compounds 1 and 2 were found to be new ones. All of them simultaneously inhibited PTP1B with IC₅₀s of (2.4–52.5 µM), and α-glucosidase with IC₅₀ values of (1.7–72.7 µM), respectively. Cratoxanthone A (3) and γ-mangostin (7) were estimated to be most active inhibitors against both PTP1B (IC₅₀ = 2.4 µM for 3, 2.8 µM for 7) and α-glucosidase (IC₅₀ = 4.8 µM for 3, 1.7 µM for 7). In kinetic studies, all isolated xanthones emerged to be mixed inhibitors of α-glucosidase, whereas they behaved as competitive inhibitors of PTP1B. In time dependent experiments, compound 3 showed isomerization inhibitory behavior with following kinetic parameters: K_i^app = 2.4 µM; k₅ = 0.05001 µM⁻¹ S⁻¹ and k₆ = 0.02076 µM⁻¹ S⁻¹.

Cratoxylum cochinchinense对蛋白酪氨酸磷酸酶 1B (PTP1B) 和 α-葡萄糖苷酶具有显着抑制作用，这两种酶都是减轻糖尿病和肥胖症的关键靶酶。负责这两种酶抑制的化合物被确定为十二个氧杂蒽酮 ( 1-12 ) ，其中化合物1和2被发现是新化合物。它们同时抑制 PTP1B，IC ₅₀ s 为 (2.4–52.5 µM)，α-葡萄糖苷酶抑制 IC ₅₀值分别为 (1.7–72.7 µM)。据估计， Cratoxanthone A ( 3 ) 和 γ-mangostin ( 7 ) 是对 PTP1B (IC ₅₀ = 2.4 µM for 3 , 2.8 µM for 7 ) 和 α-葡萄糖苷酶 (IC ₅₀  = 4.8 µM for 3 , 1.7 µM for 7 )。在动力学研究中，所有分离的呫吨酮都是 α-葡萄糖苷酶的混合抑制剂，而它们表现为 PTP1B 的竞争性抑制剂。在时间依赖性实验中，化合物3显示出异构化抑制行为，具有以下动力学参数：K _i ^app  = 2.4 µM；k ₅  = 0.05001 µM ^-1  S ^-1和k ₆  = 0.02076 µM ^-1  S ^-1。