Risteli J, Tuderman L, Kivirikko K I
Biochem J. 1976 Aug 15;158(2):369-76. doi: 10.1042/bj1580369.
Prolyl hydroxylase was purified from newborn rats by affinity chromatography using poly(L-proline), and antiserum to the enzyme was prepared in rabbits. The rat prolyl hydroxylase was similar to the chick and human enzymes with respect to specific activity, molecular weight and molecular weights of the polypeptide chains. The activity of prolyl hydroxylase and the content of immunoreactive enzyme were measured in rat liver as a function of age in experimental hepatic injury. Active prolyl hydroxylase comprised about 13.2% of the total immunoreactive protein in the liver of newborn rats and the value decreased to about 3.6% at the age of 420 days. This decrease was due to a decrease in the enzyme activity, whereas only minor changes were found in the content of the immunoreactive protein. In hepatic injury, a significant increase was found in the ratio of active enzyme to total immunoreactive protein, owing to an increase in the enzyme activity. The data indicate that prolyl hydroxylase activity in rat liver is controlled in part by a mechanism which does not involve changes in the content of the total immunoreactive protein.
利用聚（L-脯氨酸）通过亲和层析从新生大鼠中纯化出脯氨酰羟化酶，并在兔体内制备了该酶的抗血清。大鼠脯氨酰羟化酶在比活性、分子量和多肽链分子量方面与鸡和人源的酶相似。在实验性肝损伤中，测定了大鼠肝脏中脯氨酰羟化酶的活性以及免疫反应性酶的含量随年龄的变化。活性脯氨酰羟化酶约占新生大鼠肝脏中总免疫反应性蛋白的13.2%，在420日龄时该值降至约3.6%。这种下降是由于酶活性降低所致，而免疫反应性蛋白的含量仅发生了微小变化。在肝损伤中，由于酶活性增加，活性酶与总免疫反应性蛋白的比值显著升高。数据表明，大鼠肝脏中脯氨酰羟化酶的活性部分受一种不涉及总免疫反应性蛋白含量变化的机制控制。
