ArticleFischer J, Heyer W, Janowski F, Wolf F, Schellenberger A.
Acta Biol Med Ger. 1977;36(7-8):999-1005.
Macroporous glasses with pore sizes from 400-1000 A appropriate for protein binding were produced and characterized by a thermal demixing procedure and alkaline after treatment. To achieve a covalent binding capacity relative to proteins, the gamma-aminopropyl derivative was allowed to react with 4-maleinimido benzoylic chloride to give preparations containing, in addition to maleinimide residues, acid chloride structures for the protein binding. A preparation of 400 A pore size was tested for its protein binding capacity relative to bovine serum albumin and trypsin. Furthermore, the capacity of binding glucoamylase from Endomycopsis bispora in active form was studied.