Abstract
1. Radioisotope incorporation studies of normal and lathyritic chick embryo bone collagen do not demonstrate any interference by lathyrism with collagen synthesis or fibril formation. 2. The results indicate that a portion of the extractable collagen from lathyritic chick embryo bone represents newly synthesized protein. Evidence from a double labeling experiment and from analysis of isotope flow between the extractable and non-extractable pools suggests the extractable lathyritic collagen is heterogeneous. We propose that the lathyritic process affects collagen in all states of aggregation, probably in varying degree. 3. Puromycin, administered intravenously, reduces the amount of extractable collagen in both normal and lathyritic chick embryo bone, and diminishes the incorporation of labeled proline into collagen. 4. Marked fluctuations in incorporation of labeled amino acids into chick embryo bone collagen suggests the occurrence of wide fluctuations in metabolism of this protein.
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