The fine structure of normal rat aorta in experimental lathyrism.
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In normal and lathyritic chick embryos bone collagen was synthesized primarily in the periosteum of the femurs, and was organized as radioactive spicules in these bones. Saline extraction of the lathyritic bones removed the radioactive spicules, although they eventually seemed to become non-extractable. Normal bone seemed to be unaffected by saline extraction. Marked variation in the degree of isotope incorporation was seen in collagenous and non-collagenous tissues. All the tissues of any one embryo, however, showed a similar degree of isotope incorporation. Tritiated beta-aminopropionitrile was diffusely distributed throughout bone and was completely removed by saline extraction. This autoradiographic study supports the postulate that a portion of extractable lathyritic collagen is recently synthesized and is organized in fibrous structures in bone.
1. C(14)-labeled beta-aminopropionitrile distributed throughout the egg contents within 10 minutes postinjection. By ion exchange chromatography and electrophoretic analysis three major components of the extractable dialyzable radioactive material could be demonstrated, representing at least 80 per cent of the total. The acidic and basic components were identified as beta-aminopropionitrile and cyanoacetic acid, while the fraction isoelectric at pH 5.3, consisting of two components, remained unidentified. 2. Less than 1 molecule of betaAPN per 100 molecules of protein was present in the highly purified extractable lathyritic bone collagen indicating that binding of the lathyrogen is not a factor in collagen extractability. 3. The proximity of betaAPN to collagen in bone is not essential to its extractability. 4. The effect of incubation temperature of the embryo on collagen extractability suggests the involvement of a metabolic process in this phenomenon.
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