Work

Methionyl Soluble Ribonucleic Acid Transformylase

Year: 1967

Type: article

Abstract: 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.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)96123-5

Authors: Herbert W. Dickerman, Edward Steers, Betty G. Redfield, Herbert Weissbach

Institutions: National Institutes of Health, National Heart Institute, National Heart Institute, National Heart Institute

Language: English

Topic: RNA and protein synthesis mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1536603220

FWCI: 6.924

Cites: 14

Cited by: 128

Related to: 10