Crane D, Holmes R, Masters C
Int J Biochem. 1983;15(12):1429-37. doi: 10.1016/0020-711x(83)90075-7.
The processes associated with the biogenesis of peroxisomes in mouse liver have been studied by following the incorporation of radiolabelled leucine into major enzymic components of this organelle. Maximal incorporation of label into peroxisomal catalase and urate oxidase occurred within 2 hr, with the urate oxidase being labelled before catalase, but subsequent to the incorporation of phospholipid into this organelle. Subsequently, immunoprecipitation of catalase from the large granular fraction of mouse liver was shown to result in the isolation of a catalase molecule which had lost a peptide of approx. 2000 dalton from each subunit by comparison with the newly-synthesized enzyme. It was observed that the modification of catalase was obviated by the presence of leupeptin and iodoacetamide and this information has enabled the purification of both modified and unmodified forms of the enzyme. The possible significance of these data has been discussed and the major features incorporated into a working model of peroxisomal biogenesis.
通过追踪放射性标记的亮氨酸掺入小鼠肝脏中该细胞器的主要酶成分，对与过氧化物酶体生物发生相关的过程进行了研究。标记物在2小时内最大程度地掺入过氧化物酶体过氧化氢酶和尿酸氧化酶中，尿酸氧化酶在过氧化氢酶之前被标记，但在磷脂掺入该细胞器之后。随后，从小鼠肝脏的大颗粒部分免疫沉淀过氧化氢酶，结果显示分离出的过氧化氢酶分子与新合成的酶相比，每个亚基失去了一个约2000道尔顿的肽段。观察到亮肽素和碘乙酰胺的存在可避免过氧化氢酶的修饰，这一信息有助于纯化该酶的修饰形式和未修饰形式。已经讨论了这些数据可能的意义，并将主要特征纳入了过氧化物酶体生物发生的工作模型中。
