Paxton J W, Jurlina J L, Foote S E
J Pharm Pharmacol. 1986 Jun;38(6):432-8. doi: 10.1111/j.2042-7158.1986.tb04606.x.
Determination of amsacrine plasma protein binding by both equilibrium dialysis and ultracentrifugation gave similar results and indicated that amsacrine is highly bound (approximately 97%) in human plasma. This binding is independent of amsacrine concentration over the range 1-100 mumol litre-1, but is very sensitive to plasma pH and, to a lesser extent, to temperature. Approximately 20% of the drug appeared to be covalently bound to plasma proteins. Amsacrine was bound by all plasma proteins investigated including albumin, alpha 1-acid glycoprotein and various gamma-globulins. The binding to albumin appeared to occur by two processes, a saturable process at a single site with a KD of 13.9 mumol litre-1 and a non-saturable process. Despite differences in individual protein concentrations, no significant difference was observed in the unbound amsacrine fraction in plasma from patients receiving this drug for treatment of acute myelogenous leukaemia and plasma from healthy individuals.
通过平衡透析和超速离心法测定安吖啶与血浆蛋白的结合情况，结果相似，表明安吖啶在人血浆中高度结合（约97%）。在1 - 100μmol/L的浓度范围内，这种结合与安吖啶浓度无关，但对血浆pH非常敏感，对温度的敏感性稍低。约20%的药物似乎与血浆蛋白共价结合。安吖啶与所有研究的血浆蛋白结合，包括白蛋白、α1 - 酸性糖蛋白和各种γ - 球蛋白。与白蛋白的结合似乎通过两个过程发生，一个是在单一部位的可饱和过程，KD为13.9μmol/L，另一个是非饱和过程。尽管个体蛋白浓度存在差异，但在接受该药物治疗急性髓性白血病的患者血浆和健康个体血浆中，未结合的安吖啶分数未观察到显著差异。
