Immobilization of Low-Cost Alternative Vegetable Peroxidase ( L. peroxidase): Choice of Support/Technique and Characterization.

In the present work the radish ( L.) was used as the low-cost alternative source of peroxidase. The enzyme was immobilized in different supports: coconut fiber (CF), calcium alginate microspheres (CAMs) and silica SBA-15/albumin hybrid (HB).

(99m)Tc complexes with activated ester functions; ligands comprising a 3,4-diamino-benzoate backbone.

Preformed (99m)Tc chelates with an activated ester function are useful for the gentle labeling of proteins (precomplexation route). In this context, new heterobifunctional ligands derived from 2,3,5,6-tetrafluorophenyl (TFP) 3,4-diamino-benzoates (OC1, OC3, OC4) were synthesized. Their corresponding (99m)Tc-complexation and protein-conjugation characteristics were elucidated and compared with the results previously reported using 2,3,5,6-tetrafluorophenyl N-(S-benzoylthioacetyl)glycylglycyl-p-aminobenzoate (OC2).