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. 1969 Mar;62(3):928–933. doi: 10.1073/pnas.62.3.928

TRANSLOCATION OF MRNA CODONS, II. PROPERTIES OF AN ANTI-TRANSLOCASE ANTIBODY

Philip Leder 1, Lawrence E Skogerson 1, Donald J Roufa 1
PMCID: PMC223687  PMID: 4895218

Abstract

A purified preparation of translocase, one of several enzymes required for protein biosynthesis, has been used to prepare a specific anti-translocase antibody. This antibody provides an extremely useful tool not only for detecting the enzyme independent of its activity, but for inhibiting the translocase-mediated reaction and, thus, protein biosynthesis. Though the antibody very rapidly inhibits elongation of the peptide chain, it fails to effect initiation, binding, or peptide bond formation, which strongly suggests that translocase is not a direct participant in these reactions. It also arrests translation of the defined tricodon AUG(U6) at the second codon, permitting formation only of the dipeptide, fMet-Phe, rather than the tripeptide, fMetPhe-(Phe)2, which is formed in the presence of control serum. We have shown previously that the third codon becomes available only in the presence of translocase, thereby defining the site of action of the antibody. The antibody also has been used to demonstrate that translocase is antigenically distinct from the other proteins required for initiation and protein synthesis in E. coli.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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