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The chelator EDTA is often added to buffers that are used to isolate and purified proteins...

The chelator EDTA is often added to buffers that are used to isolate and purified proteins to inhibit proteases. Explain which family of proteases is going to be inhibited by EDTA and why.

a) Asp proteases

b) metalloproteases

c) Ser proteases

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Answer #1

Question- The chelator EDTA is often added to buffers that are used to isolate and purified proteins to inhibit proteases. Explain which family of proteases is going to be inhibited by EDTA and why?

Answer- Metalloproteases

Metalloproteases are the proteases that consists metal ions such as zinc (Zn2+), cobalt (CO2+), manganese (Mn2+) at the active site of the enzyme that act as catalysts for breaking (hydrolysis) of the peptide bonds.

EDTA acts as a chelator of divalent metal ions zinc (Zn2+), cobalt (CO2+), manganese (Mn2+). It minimizes metal ion contamination and prevent enzymatic activity. Therefore, EDTA chelates the divalent metal ions and inhibits its activity of hydrolysis of peptide bond.

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