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Disulfide bonds are required for Serratia marcescens nuclease activity.

Nucleic acids research (1992-10-11)
T K Ball, Y Suh, M J Benedik
RESUMEN

The role of the two disulfide bonds found in the Serratia marcescens nuclease were tested by site directed mutagenesis and were found essential for nuclease activity, although slight residual activity remained. The requirement for disulfide bond formation may play a role in preventing the lethal action of nuclease while in the bacterial cytoplasm.

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Millipore
Nucleasas Benzonase®, ≥250 units/μL, ≥90% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution
Sigma-Aldrich
Nucleasas Benzonase® ultrapuras, ≥250 units/μL, ≥99% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution, ultrapure grade