The Small Metal-Binding Protein SmbP Improves the Expression and Purification of the Recombinant Antitumor-Analgesic Peptide from the Chinese Scorpion Karsch in .

We have recently shown that SmbP, the small metal-binding protein of , can be employed as a fusion protein to express and purify recombinant proteins and peptides in . SmbP increases solubility, allows simple, one-step purification through affinity chromatography, and provides superior final yields due to its low molecular weight. In this work, we report for the first time the use of SmbP to produce a recombinant peptide with anticancer activity: the antitumor-analgesic peptide (BmK-AGAP), a neurotoxin isolated from the venom of the Chinese scorpion Karsch.

Enhanced in vitro anticancer activity of yeast expressed recombinant glucose oxidase versus commercial enzyme.

Cancer treatments continue to have many disadvantages. Reactive oxygen species, such as HO, in high concentrations, can cause cytotoxicity to cells, being even greater in cancer cells. One of the HO-producing enzymes is glucose oxidase; its application in cancer treatment should be explored.