Abstract
Two questions that are often raised in connection with the biosynthesis of macromolecules, such as proteins, are:
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1.
When amino acid incorporation is measured in the absence of net synthesis, is this really measuring activity along a potential synthetic pathway, or an exchange such as might be produced by the action of a reversible hydrolytic enzyme?
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2.
Does biosynthesis of, e.g., proteins involve a template mechanism in which the entire molecule is assembled at a single site, or does it proceed by the stepwise building of ever larger intermediates?
Presented at the Fourth Symposium on Advances in Tracer Methodology, 1960.
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References
Reiner, J. M. Arch. Biochem Biophys. 46, 53, 80 (1953).
Jardetztry, C.D., and Barnum, C. P. Arch. Biochem. Biophys. 73, 435 (1958).
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© 1963 New England Nuclear Corporation
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Reiner, J.M. (1963). Experimental Design of Turnover Measurement Studies in the Unsteady State: Biosynthesis of Macromolecules. In: Rothchild, S. (eds) Advances in Tracer Methodology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8619-3_37
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DOI: https://doi.org/10.1007/978-1-4684-8619-3_37
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