Cyclosporin synthetase is a 1.4 MDa multienzyme polypeptide Re‐evaluation of the molecular mass of various peptide synthetases

FEBS Letters

Riesner, Detlev¹  Lawen, Alfons²  Schmidt, Bettina¹  Kleinkauf, Horst² 

[1] Institut für Physikalische Biologie, Heinrich-Heine Universität Düsseldorf, Universitätsstr. 1, D-(W)-4000 Düsseldorf, Germany;Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, Franklinstr. 29, D-(W)-1000 Berlin 10, Germany

关键词: Cyclosporin synthetase;    SDS-PAGE;    Analytical ultracentrifugation;    Fluorescence;    Peptolide SDZ 214-103 synthetase;    Sedimentation coefficient;    ACV;    δ-(l-α-aminoadipyl)-l-cysteinyl-d-valine;    CyA;    cyclosporin A;    IAMF;    4′-(((iodoacetyl)amino)methyl)fluorescein;   

DOI  :  10.1016/0014-5793(92)80712-P

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 extremly 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.

【 授权许可】

Unknown