Schmidt B, Riesner D, Lawen A, Kleinkauf H
Institut für Physikalische Biologie, Heinrich-Heine Universität Düsseldorf, Germany.
FEBS Lett. 1992 Aug 3;307(3):355-60. doi: 10.1016/0014-5793(92)80712-p.
The earlier determined molecular mass of 0.8 MDa for the multifunctional polypeptide, cyclosporin synthetase, was re-evaluated by SDS-PAGE and CsCl density gradient centrifugation. In SDS-PAGE, new molecular mass values as standards were available from sequencing data. In the CsCl density gradient extremely low protein concentrations, such as 10-50 nM could be analysed due to the fluorescence detection system of the analytical ultracentrifuge. Both methods yielded approximately the same value of about 1.4 MDa. Using this molecular mass of cyclosporin synthetase as a reference the molecular masses of various related enzymes could be re-evaluated in SDS-PAGE. The sedimentation coefficient of 26.3 S for cyclosporin synthetase indicates an oblate overall shape of the enzyme.
通过SDS - PAGE和CsCl密度梯度离心法对多功能多肽环孢菌素合成酶先前测定的0.8 MDa分子量进行了重新评估。在SDS - PAGE中，可从测序数据获得作为标准的新分子量值。在CsCl密度梯度中，由于分析超速离心机的荧光检测系统，可分析极低的蛋白质浓度，如10 - 50 nM。两种方法得到的结果大致相同，约为1.4 MDa。以环孢菌素合成酶的这种分子量为参考，可在SDS - PAGE中重新评估各种相关酶的分子量。环孢菌素合成酶26.3 S的沉降系数表明该酶整体呈扁球形。
