综述了定性和定量研究药物—蛋白结合作用的部分方法，包括色谱、毛细管电泳、核磁共振光谱、质谱等方法及一些传统方法如平衡透析、超滤等方法，并讨论了各自的优点和局限性。

A method of capillary electrophoresis frontal analysis (CEFA) is developed for the first time to study the binding of ketoprofen to human serum albumin (HSA) and compared with high performance liquid chromatography frontal analysis (LCFA). The separation is performed in an uncoated fused-silica capillary (60-cm × 75-μm i.d., 50-cm effective length) with a phosphate buffer (pH 7.4, ionic strength of 0.17M) as the running buffer. The applied voltage is 13 kV and the detection is set at 254 nm. A trapezoidal peak of the unbound ketoprofen appears after HSA elution in the electropherogram. The plateau height of the peak is employed to determine the unbound concentration of ketoprofen in the HSA equilibrated sample solution. The CEFA method provides the advantages of small sample injection volume and rapidity and the disadvantage of low sensitivity compared with LCFA. CEFA is applicable to the binding parameter estimation of ketoprofen to the secondary binding site; an association c:onstant (K2) of 0.24 × 106M-1 and the number for the binding site per molecule HSA of 2.54 is estimated. In contrast, LCFA measures parameters for both primary and secondary sites, which are 1.05 ×106M-l and 0.94 for K1 and n1, respectively, and 0.12 × 106M-1 and 3.16 for K2 and n2, respectively. It is found that ketoprofen binds mainly at the primary site at a molecular ratio of ketoprofen versus HSA lower than 0.75, and the binding at the secondary site occurs at a higher ratio.

报道了双（1- 正戊基环己基茂）二氯化钛[(η5- C5H4C(CH2)5(C5H11- n)]2TiCl2(Ⅰ)及双（1- 甲基- 1-（α- 噻吩基）乙基环戊二烯基）二氯化钛[η5- C5H4C(CH3)2- ？？]2TiCl2(Ⅱ)的晶体结构和分子结构。二者均系单斜晶系，（Ⅰ）的空间群为P2/ n，晶胞参数a= 14.180(2)，b= 6.562(1)，c= 17.046(3) A，β= 99.63(1)°，Z= 2，V= 1563.8 A3，Dx= 1.188 g/ cm3，F(000)= 596，Mr= 553.56，λ= 0.71073 A，μ=4.59 cm-1，R= 0.058，Rw= 0.066；(Ⅱ)的空间群为C2/ c，晶胞参数a= 25.713(1)，b= 6.617(1)，c= 13.591(1) A，β= 92.78(2)°，Z= 4，V= 2309.8 A3, Dx= 1.430 g/ cm3，Mr= 497.41，λ= 0.71073 A．μ= 7.822 cm-1，F(000)= 1032，R= 0.055，Rw= 0.072。茂环上取代基对茂环金属化合物的结构产生较大影响，空间阻碍的增大使得取代基与茂环相连C- C单键增长。

目的 研究格列美脲与人血清白蛋白（human serum albumin, HSA）结合作用。方法 采用高效液相色谱—迎头分析法（high performance liquid chromatography- frontal analysis, HPLC- FA）。色谱柱为内表面反相（internal- surface reversed- phase, ISRP）硅胶柱Pinkerton GFF Ⅱ- S5- 80(150 mmx 4.6 mm ID, 5 μm)；流动相为67 mmol·L-1磷酸盐等渗缓冲液(pH 7.4, I= 0.17 mol·L-1)；流速0.2 mL·min-1；检测波长230 nm；进样量900 μL；柱温37℃。结果应用非线性回归参数估算求得HSA分子上两类结合位点结合的格列美脲分子数及相应的结合平衡常数：n1= 1和K1= 5.1(μmol·L-1)-1；n2= 7和K2= 0.017(μmol·L-1)-1。结论 HPLC- FA法操作简便，适用于研究格列美脲与HSA的结合作用。

将18- 甲基炔诺酮加到人血清白蛋白—酮洛芬平衡溶液中，室温孵育达平衡后应用毛细管电泳—迎头分析法研究了18- 甲基炔诺酮和酮洛芬在人血清白蛋白分子上的置换相互作用。—大体积样品虹吸进样至未涂层毛细管(65 cm×50μm i. d., 有效长度35 cm)，进样时间80 s，毛细管两端高度差11 cm，工作电压10 kV，运行缓冲液为67 mmol/ L磷酸盐缓冲液(pH 7.4)，游离酮洛芬浓度由前沿峰的高度直接测定。当酮洛芬样品溶液中酮洛芬的总浓度分别为100 μmol/ L和200 μmol/ L时，随着18- 甲基炔诺酮加入量的增加（18- 甲基炔诺酮的浓度由0增至200μmol/ L），游离酮洛芬的浓度分别从22.4增至26.4 μmol/ L和从82.1增至106.2 μmol/ L。由上面的结果可推论：高浓度的18- 甲基炔诺酮可将酮洛芬从它的第二类结合位点上置换出来。