顺式二氯二氨合铂（II）对人纤维蛋白原二硫键的裂解
Disulfide bond cleavage of human fibrinogen by cis-diamminedichloroplatinum(II).
作者信息
Ohta N, Yotsuyanagi T, Ikeda K
机构信息
Faculty of Pharmaceutical Sciences, Nagoya City University, Japan.
出版信息
J Pharmacobiodyn. 1992 Nov;15(11):611-5. doi: 10.1248/bpb1978.15.611.
Disulfide bridges in fibrinogen (Fbg) were cleaved by cis-diamminedichloroplatinum(II) (cis-DDP). Incubation with 120 molar excess of cis-DDP at pH 7.4 and 37 degrees C in the presence of EDTA resulted in cleavage of seven disulfide bridges out of 29. In the presence of calcium, however, the number of cleavages were reduced to four. The result indicates that calcium, which has three high affinity sites on Fbg, protects disulfide bridges from the rupture. Thrombin clottability was examined by turbidity measurement. The cis-DDP treated Fbg was shown to give a decreased fiber thickness. As the cleavage proceeded, the clotting ability of Fbg decreased.
纤维蛋白原（Fbg）中的二硫键被顺二氯二氨铂（II）（顺铂）裂解。在pH 7.4、37摄氏度且存在乙二胺四乙酸（EDTA）的条件下，用120摩尔过量的顺铂孵育，导致29个二硫键中有7个被裂解。然而，在有钙存在的情况下，裂解的数量减少到4个。结果表明，在Fbg上有三个高亲和力位点的钙可保护二硫键不被断裂。通过比浊法测量来检测凝血酶的可凝性。结果显示，经顺铂处理的Fbg纤维厚度减小。随着裂解过程的进行，Fbg的凝血能力下降。
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