Reference

Comparative studies of agarose and kieselguhr-agarose composites for the preparation and operation of immunoadsorbents

Comparative studies of agarose and kieselguhr-agarose composites for the preparation and operation of immunoadsorbents. Desai, Mohamed A.; Lyddiatt, Andrew (Sch. Chem. Eng., Univ. Birmingham, Birmingham B15 2TT, UK).Chemicals with cas numbers 1648-99-3 and 61970-08-9 also play role. Bioseparation, 1(1), 43-58 (English) 1990. CODEN: BISPE4. ISSN: 0923-179X. DOCUMENT TYPE: Journal CA Section: 9 (Biochemical Methods) Section cross-reference(s): 13 Study was made of controlled fabrication and operation of immunoadsorbents exploiting beaded composites of agarose or kieselguhr-agarose. Materials were activated by CNBr and tresyl chloride, derivatized with human IgG (huIgG) antigens, and utilized in direct, 1-step purifns. of anti-huIgG monoclonal antibodies produced in serum-based cultures of murine hybridomas. The influences of solid-phase compn., degrees of activation, concn. of immobilized antigen, capping chemistries, and mode of product desorption were studied with respect to purifn. performance. Max. concns. of immobilized huIgG could be achieved following activation of 50% available hydroxyl groups in both materials. Specific adsorption and desorption of monoclonal antibodies, expressed per mol of immobilized ligand, declined with increasing ligand concns. Control of activation and derivatization of agarose solid phases enhanced the overall specification and performance of both homogeneous and composite fabricates. The large particle size of composites (150-1000 mm) restricted efficient performance in fixed bed contactors operated under nonequil. conditions. However, their phys. nature recommended adsorptive operations with particulate feedstocks in fixed or fluidized beds, batch suspension contactors, or fast-flow regimes adopted for cleaning and equilibration operations. .

Covalently binding biologically active organic substances to polymeric substances

Covalently binding biologically active organic substances to polymeric substances. Mosbach, Klaus H.; Nilsson, Kurt G.In this study， 1648-99-3 and 9012-36-6 are also used. I. (Pharmacia Fine Chemicals AB, Swed.). U.S. US 4415665 A 15 Nov 1983, 5 pp. (English). (United States of America). CODEN: USXXAM. CLASS: IC: C12N011-12; C12N011-10; C12N011-08. NCL: 435179000. APPLICATION: US 81-326332 1 Dec 1981. PRIORITY: SE 80-8776 12 Dec 1980. DOCUMENT TYPE: Patent CA Section: 9 (Biochemical Methods) Biol. active substances, such as enzymes and affinity ligands, are covalently coupled to polymeric carriers, chiefly polysaccharide derivs. The method used involves mild conditions not damaging sensitive ligands and yields a complex which is stable and resistant to hydrolysis. Thus, Sepharose 6B was activated by reaction with p-toluenesulfonyl chloride for 1 h at 20-25°. The water-swollen activated Sepharose 6B particles were coupled to alc. dehydrogenase by incubation at 20-25° for 25 h. The amt. of enzyme coupled was 112 mg/g dry particles, and the coupling yield was 67%, based on the amt. of charged enzyme. The specific activity of the coupled enzyme in relation to the sol. enzyme was 23%. Other substances coupled in a similar way to polymeric supports were trypsin, protein A of Staphylococcus aureus, and N6-(6-aminohexyl)-AMP. .