Studies on the effect of l-3,4-dehydroproline on collagen synthesis by chick embryo polysemes |
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Authors: | S.S. Kerwar Richard J.M. Marcel Richard A. Salvador |
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Affiliation: | Roche Institute of Molecular Biology, Nutley, New Jersey 07110 USA;Department of Pharmacology, Hoffmann-La Roche Inc., Nutley, New Jersey 071101 USA |
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Abstract: | Various proline analogs have been tested in vitro for their ability to inhibit the enzymatic aminoacylation of tRNA by proline. Of these, l-3,4-dehydroproline is the most potent inhibitor. This inhibition is competitive; the Ki is 100 μm. It was shown that l-3,4-dehydroproline can serve as substrate in the aminoacylation reaction. However, the incorporation of radioactivity from l-3,4-[14C]dehydroprolyl-tRNA into protein occurs at one-fifth the rate observed for l-prolyl-tRNA. The addition of l-3,4-dehydroproline in vitro inhibits the synthesis of collagen to a greater extent than non-collagen protein. |
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Keywords: | All correspondence to the author's present address: Division of Metabolic Diseases CIBA-Geigy Ardsley N. Y. 10502. |
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