A novel, facile, and robust strategy was proposed to increase the pore size and mechanical strength of cryogels. By mixing the monomers of acrylamide and 2‐hydroxyethyl methacrylate as the precursor, a monolithic copolymer cryogel with large interconnected pores and thick pore walls was prepared. Hydrogen bonding between the two monomers contributed to the entanglement and aggregation of the copolymers, thickening the pore walls and resulting in larger pore sizes. Analysis via mercury porosimetry demonstrated that the interconnected pore diameter of the copolymer cryogel ranged from 10‐350 µm, which was far larger than that of the cryogels from one monomer (10‐50 µm). Additionally, the thicker pore walls of the copolymer cryogel improved its mechanical strength. Affinity cryogels were prepared through covalent immobilization using Tris(hydroxymethyl)aminomethane as a coupling agent, and the affinity binding of lysozymes on Tris‐cryogel was evaluated by the Langmuir isothermal adsorption with the maximum adsorption capacity of 360 mg/g. Compared with that of the Tris‐cryogels produced from one monomer, the copolymer Tris‐cryogel exhibited higher adsorption capacity and lysozyme purity, when the chicken egg white solution flowed solely driven by gravity. This work provides a new avenue for designing and developing supermacroporous cryogels for bioseparation.
Reaction of [Mn 12 (CH 3 COO) 16 (H 2 O) 4 O 12 ]Á2CH 3 COOHÁ4H 2 O and Na 9 [AsW 9 O 33 ]Á19.5H 2 O in aqueous solution leads to the isolation of a new carboxy group decorated TMSP, Na 15 [(Mn II (COOH)) 3 (AsW 9 O 33 ) 2 ]Á15H 2 O (1). The structure of 1 was characterized by elemental analysis, thermometric analysis and single crystal X-ray diffraction (Crystal data for 1: Trigonal, P-3, a = 12.8804(4) Å , b = 12.8804(4) Å , c = 30.3501(19) Å , V = 4360.6(3) Å 3 , Z = 2). Structural analysis reveals that 1 represents the first example of carboxy group decorated arsenotungstate. Antitumor study indicates that compound 1 possesses high antitumor activity against Hela cells. In addition, the magnetic properties of 1 were also investigated.Electronic supplementary material The online version of this article (
The eigenvectors of a fuzzy matrix correspond to steady states of a complex discrete-events system, characterized by the given transition matrix and fuzzy state vectors. The descriptions of the eigenspace for matrices in the max-Łukasiewicz algebra, max-min algebra, max-nilpotent-min algebra, max-product algebra and max-drast algebra have been presented in previous papers. In this paper, we investigate the monotone eigenvectors in a max-T algebra, list some particular properties of the monotone eigenvectors in max-Łukasiewicz algebra, max-min algebra, max-nilpotent-min algebra, max-product algebra and max-drast algebra, respectively, and illustrate the relations among eigenspaces in these algebras by some examples.
The poor reactivity between proteins and epoxy agarose gels limits studies of many protein‐agarose conjugates. We present here a novel and simple strategy for oriented covalent immobilization of recombinant protein A (rSpA) on epoxy agarose gels. The method can be basically considered as an immobilization of proteins on the heterofunctional amino‐epoxy agarose gels generated in situ. The epoxy agarose gel was directly incubated with rSpA solution containing ethylenediamine (EDA). The presence of EDA during immobilization permits the generation of an in‐situ heterofunctional amino‐epoxy agarose gel, which permits the ion exchange of rSpA and the following covalent reaction with the epoxy groups. The immobilization efficiency of more than 90% could be achieved by controlling the EDA concentration and pH. Interestingly, the obtained rSpA‐agarose conjugates (rSpA@Aga) using the strategy exhibits approximately 20% higher human IgG‐binding capacity than those through the immobilization of rSpA on the heterofunctional amino‐epoxy agarose gel. Moreover, the resultant rSpA@Aga can selectively adsorb Fc type antibodies and hardly adsorb albumin. Therefore, an effective strategy to develop a high IgG‐binding adsorbent is provided, showing potential applications for hemoperfusion in blood purified therapy.
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