Nwagwu M, Reid S A
Biochem J. 1977 Aug 15;166(2):199-204. doi: 10.1042/bj1660199.
Radioactive protein was prepared from the leg muscle of chick embryos, 11, 14, 16 and 17 days old, each injected with radioactive proline and incubated for 30, 60 or 90 min afterwards. The radioactive protein was incubated with collagenase purified by chromatography on a Sephadex G-100 column. Under this condition, only collagen is digested into products soluble in trichloroacetic acid. The relative rate of collagen synthesis was determined by comparing the amount of radioactivity released into the supernatant fraction and that in the residue, by the method of Diegelmann & Peterkofsky [(1972) Dev. Biol. 28, 443--453]. The results show that the rate of collagen synthesis remains at approx. 10% of the rate of synthesis of other non-collagenous proteins during the development of chick embryonic muscle from 11 to 17 days. This suggests that the synthesis of collagen and that of other proteins are co-ordinately regulated at these stages of development.
放射性蛋白质是从11、14、16和17日龄鸡胚的腿部肌肉制备的，每个鸡胚均注射放射性脯氨酸，然后孵育30、60或90分钟。将放射性蛋白质与通过Sephadex G - 100柱层析纯化的胶原酶一起孵育。在这种条件下，只有胶原蛋白被消化成可溶于三氯乙酸的产物。通过比较释放到上清液部分和残渣中的放射性量，采用迪格尔曼和彼得科夫斯基的方法[(1972)《发育生物学》28, 443 - 453]来测定胶原蛋白合成的相对速率。结果表明，在11至17日龄鸡胚肌肉发育过程中，胶原蛋白合成速率约为其他非胶原蛋白合成速率的10%。这表明在这些发育阶段，胶原蛋白的合成与其他蛋白质的合成是协同调控的。
