Direct in vitro effects of bis(tri-n-butyltin)oxide on hepatic cytochrome P-450.
Direct in vitro effects of bis(tri-n-butyltin)oxide on hepatic cytochrome P-450.
复制标题
双（三正丁基锡）氧化物对肝细胞色素 P-450 的直接体外影响。
DOI：
10.1016/0006-2952(83)90155-7
复制
发表时间：
1983
影响因子：
5.8
通讯作者：
Drummond,GS
中科院分区：
文献类型：
--
作者：
Rosenberg,DW;Drummond,GS
双（三正丁基锡）氧化物，一种农业上重要的杀生物剂，当在体外加入到含有苯巴比妥诱导形式的细胞色素P-450的肝微粒体中时，产生典型的I型结合光谱（最大吸收在390 nm处;最小吸收在420 nm处）。对含有细胞色素P-448的微粒体制备物进行的研究表明，与未诱导或苯巴比妥诱导形式的细胞色素P-450相比，该血红素蛋白更容易被双（三正丁基锡）氧化物直接降解。光谱可检测的细胞色素P-450的消失伴随着细胞色素P-420的增加。细胞色素P-420的形成是时间和温度依赖性的，它也发生在更大程度上在微粒体制剂含有细胞色素P-448比微粒体含有苯巴比妥诱导的细胞色素P-450的形式。在所有情况下，减少光谱检测细胞色素P-450产生的有机锡并不伴随着减少微粒体血红素或cytochromeb 5含量。研究结果提供了证据的直接相互作用，然后由三烷基锡化合物体外产生的细胞色素P-450的细胞色素P-420的转换，并表明，不同的降解能力存在不同的亚种内的血红素蛋白。
Bis(tri-n-butyltin)oxide, an agriculturally important biocidal agent, when addedin vitroto liver microsomes containing the phenobarbital-induced form of cytochrome P-450, produced a typical type I binding spectrum (an absorption maximum at 390 nm; an absorption minimum at 420 nm). Studies with microsomal preparations containing cytochrome P-448, induced by 3-methylcholanthrene or β-naphthoflavone, revealed that this hemeprotein was more susceptible to direct degradation by bis (tri-n-butyltin)oxide than was the uninduced or phenobarbital-induced forms of cytochrome P-450. The disappearance of spectrally detectable cytochrome P-450 was accompanied by an increase in cytochrome P-420. The formation of cytochrome P-420 was both time and temperature dependent, and it also occurred to a greater extent in microsomal preparations containing cytochrome P-448 than in microsomes containing the phenobarbital-induced form of cytochrome P-450. In all cases, the decreases in spectrally detectable cytochrome P-450 produced by the organotin were not accompanied by decreases in microsomal heme or cytochromeb5content. The findings provide evidence for the direct interaction followed by conversion of cytochrome P-450 to cytochrome P-420 produced by a trialkyltin compoundin vitro, and indicate that different susceptibilities to degradation exist within the various subspecies of this hemeprotein.