Influence of protein and stationary phase properties on protein-matrix-interaction in cation exchange chromatography.

A large number of different stationary phases for ion-exchange chromatography from different manufacturers are available, which vary significantly in a number of chemical and physical properties. As a consequence, binding mechanisms may be different as well. In the work reported here, the retention data of model proteins (lysozyme, cytochrome c and two monoclonal antibodies) were determined for nine commercially available cation-exchange adsorbents.

Cation-exchange chromatography of monoclonal antibodies: characterisation of a novel stationary phase designed for production-scale purification.

A novel cation-exchange resin, Eshmuno™ S, was compared to Fractogel® SO3(-) (M) and Toyopearl GigaCap S-650M. The stationary phases have different base matrices, and carry specific types of polymeric surface modifications. Three monoclonal antibodies (mAbs) were used as model proteins to characterize these chromatographic resins.

Two alternative starter modules for the non-ribosomal biosynthesis of specific anabaenopeptin variants in Anabaena (Cyanobacteria).

Anabaenopeptins are a diverse family of cyclic hexapeptide protease inhibitors produced by cyanobacteria that contain a conserved ureido bond and D-Lys moiety. Here we demonstrate that anabaenopeptins are assembled on a nonribosomal peptide synthetase enzyme complex encoded by a 32 kb apt gene cluster in the cyanobacterium Anabaena sp. strain 90.