The carboxyl terminus heptapeptide of the R2 subunit of mammalian ribonucleotide reductase inhibits enzyme activity and can be used to purify the R1 subunit

FEBS Letters

Spanevello, Rolando A.¹  Cooperman, Barry S.¹  Hirschmann, Ralph¹  Celiker, Incila¹  Rubin, Harvey²  Yang, Fu-De¹ 

[1] Department of Chemistry University of Pennsylvania, Philadelphia, PA 19104, USA;Department of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA

关键词: Ribonucleotide reductase;    Peptide inhibition;    Affinity chromatography;    PAGE;    polyacrylamide gel electrophoresis;    RR;    ribonucleotide reductase;   

DOI  :  10.1016/0014-5793(90)80449-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The heptapeptide, FTLDADF, identical in sequence to the last seven amino acid residues of the carboxyl terminus of the R2 subunit of mouse ribonucleotide reductase (RR), and its N^α-acetyl derivative both inhibit calf thymus RR. The N^α-acetyl derivative is considerably more potent, displaying a K _i of 20 μM. The same K _i was found for N-AcFTLDADF inhibition of a reconstituted ribonucleotide reductase from calf thymus R1 and mouse R2, indicating that the C-termini of calf R2 and mouse R2 might be identical. Our results, taken together with previous results of others on inhibition of viral RR, suggest that inhibition of RRs by peptides mimicking the C-terminus of R2 may be a general phenomenon. In addition, we have shown that an affinity column, FTLDADF-Sepharose 4B, can be used to prepare ~95% pure calf thymus R1, devoid of contamination with R2, in a very simple procedure that should be generally applicable to Rl purification from many sources.

【 授权许可】

Unknown