gma-edma and 1-(3-aminopropyl)imidazole

gma-edma has been researched along with 1-(3-aminopropyl)imidazole* in 1 studies

Other Studies

1 other study(ies) available for gma-edma and 1-(3-aminopropyl)imidazole

Article	Year
Layer-by-Layer Assembly of Metal-Organic Frameworks in Macroporous Polymer Monolith and Their Use for Enzyme Immobilization. Macromolecular rapid communications, 2016, Volume: 37, Issue:6 New monolithic materials comprising zeolitic imidazolate framework (ZIF-8) located on the pore surface of poly(glycidyl methacrylate-co-ethylene dimethacrylate) monolith previously functionalized with N-(3-aminopropyl)-imidazole have been prepared via a layer-by-layer self-assembly strategy. These new ZIF-8@monolith hybrids are used as solid-phase carriers for enzyme immobilization. Their performance is demonstrated with immobilization of a model proteolytic enzyme trypsin. The best of the conjugates enable very efficient digestion of proteins that can be achieved in mere 43 s. Topics: Adsorption; Animals; Cattle; Cytochromes c; Enzymes, Immobilized; Imidazoles; Kinetics; Methylmethacrylates; Peptide Fragments; Porosity; Propanols; Proteolysis; Serum Albumin, Bovine; Surface Properties; Trypsin	2016

Article

Year

Layer-by-Layer Assembly of Metal-Organic Frameworks in Macroporous Polymer Monolith and Their Use for Enzyme Immobilization.

Macromolecular rapid communications, 2016, Volume: 37, Issue:6

New monolithic materials comprising zeolitic imidazolate framework (ZIF-8) located on the pore surface of poly(glycidyl methacrylate-co-ethylene dimethacrylate) monolith previously functionalized with N-(3-aminopropyl)-imidazole have been prepared via a layer-by-layer self-assembly strategy. These new ZIF-8@monolith hybrids are used as solid-phase carriers for enzyme immobilization. Their performance is demonstrated with immobilization of a model proteolytic enzyme trypsin. The best of the conjugates enable very efficient digestion of proteins that can be achieved in mere 43 s.

Topics: Adsorption; Animals; Cattle; Cytochromes c; Enzymes, Immobilized; Imidazoles; Kinetics; Methylmethacrylates; Peptide Fragments; Porosity; Propanols; Proteolysis; Serum Albumin, Bovine; Surface Properties; Trypsin

2016