Abstract
Salt-washed polysomes isolated from fetal or neonatal rat skin were approximately 50% as active as rabbit reticulocyte salt-washed polysomes (per A 260 unit) in the incorporation of [ 14C]leucine in a protein-synthesizing system derived entirely from rabbit reticulocytes. Rabbit reticulocyte IF-M 3 stimulated protein synthesis directed by homologous saltwashed polysomes (4- to 5-fold) and by rat skin salt-washed polysomes (3-fold). Aurintricarboxylic acid significantly inhibited protein synthesis by both types of polysomes. Incubation of the reaction products with prolyl hydroxylase from neonatal rat skin resulted in hydroxylation of [3,4- 3H]peptidyl proline, as determined by both Dowex chromatography and the formation of 3H 2O. Digestion of [ 3H]proline-labeled products with purified collagenase indicates that collagen peptides were synthesized.
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