Purification and properties of serine hydroxymethyltransferase from Sulfolobus solfataricus

Research was conducted to study the purification and characterization of serine hydroxymthyltransferase (SHMT) from the thermophilic organism Sulfolobus solfataricus. SHMT activity was determined by monitoring the rate of exchange of the alpha-hydrogen of (2-(super 3)H)glycine while a Superdex 200 column was utilized to chromatograph the enzyme from several purification steps. Results showed similarities in the size and properties of the S. solfataricus SHMT relative to procaryotic and eucaryotic SHMT.