Wendel I, Behlke J, Jänig G R
Biomed Biochim Acta. 1983;42(6):633-40.
Extended ultracentrifugation experiments have been performed on cytochrome P-450 LM2 from rabbit liver microsomes to analyse the behaviour of this membrane protein. The sedimentation coefficients and molecular weights vary between 11 S and 19 S and 350,000 and 700,000, respectively. No concentration dependence of these values could be observed between 0.3 microM 5.0 microM protein. The sedimentation coefficients and molecular weights appear to correlate with the heme content. Partial loss of heme leads to formation of aggregates of higher molecular weight. Analysis of the distribution of sedimentation coefficients clearly reveals the heterogeneity of the individual samples with values ranging from about 8 to 23 S. Thus, the smallest particle in the associate mixture of the enzyme consists of at most 3 monomers.
已对来自兔肝微粒体的细胞色素P-450 LM2进行了超离心实验，以分析这种膜蛋白的行为。沉降系数和分子量分别在11 S至19 S以及350,000至700,000之间变化。在0.3微摩尔至5.0微摩尔的蛋白质浓度范围内，未观察到这些值与浓度有关。沉降系数和分子量似乎与血红素含量相关。血红素的部分损失会导致形成更高分子量的聚集体。对沉降系数分布的分析清楚地揭示了各个样品的异质性，其值范围约为8至23 S。因此，该酶缔合混合物中最小的颗粒最多由3个单体组成。
