The study successfully purified and characterized the methionyl soluble ribonucleic acid transformylase from E. coli B, identifying its molecular weight and formyl donor.
The MO-formyltetrahydrofolate:methionyl soluble ribonucleic acid transformylase has been purified over 1500-fold from Escherichia coli B. Although not homogeneous at this stage, the enzyme was of sufficient purity to determine some physical characteristics.The sedimentation constant was 2.02 which would indicate a molecular weight of approximately 25,000.In addition to the substrates of the reaction a partial dependency on magnesium ion was observed.The identity of the formyl donor was elucidated and found to be No-formyltetrahydrofolate.
Dickerman et al. (Sat,) studied this question.
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