INTRODUCTION

Endonuclease (Serratia marcescens) is a homodimer with two 266-amino acid subunits of approximately 30 kDa each. It is produced as a recombinant enzyme in a bacterial host. The enzyme has two essential disulfide bonds. The endonuclease degrades ribonucleic acid (RNA) and deoxyribonucleic acid (DNA) through the cleavage of 3'–5' phosphodiester bonds, resulting in the formation of 5'-phosphorylated oligonucleotides that are approximately 3–5 nucleotide bases in length upon completion of the digestion process. A magnesium ion serves as a cofactor and a minimum concentration is required for endonuclease activity.