Thangaraj T, Subramanium S, Vinayakam A, Aruchami M
Department of Zoology, Konguandu Arts and Science College, Coimbatore, India.
Arch Int Physiol Biochim Biophys. 1992 Jan-Feb;100(1):79-82. doi: 10.3109/13813459209035263.
Prophenoloxidase has been successfully extracted in a stable condition from the Hemocytes of Periplaneta americana using cane sugar saline solution. Other media used to extract prophenoloxidase were found not suitable. Among the activators used (trypsin, chymotrypsin, sodium oleate and SDS), trypsin activated the proenzyme maximum. Activation during electrophoresis resulted in the dissociation of proenzyme in to two sub-units. The enzyme has also been localised by the agarose gel electrophoresis. The proenzyme was stable up to 50 degrees C and precipitated at 60 degrees C and above. The activated enzyme showed maximum activity at pH 7.0. Preliminary attempt has also been made to precipitate the enzyme protein against the antibody raised in rabbit.
已使用蔗糖盐溶液成功地从美洲大蠊血细胞中在稳定条件下提取了酚氧化酶原。发现用于提取酚氧化酶的其他介质不合适。在所使用的激活剂（胰蛋白酶、胰凝乳蛋白酶、油酸钠和十二烷基硫酸钠）中，胰蛋白酶对酶原的激活作用最大。电泳过程中的激活导致酶原解离成两个亚基。该酶也已通过琼脂糖凝胶电泳进行了定位。酶原在高达50摄氏度时稳定，在60摄氏度及以上沉淀。激活后的酶在pH 7.0时表现出最大活性。还初步尝试了用兔产生的抗体沉淀酶蛋白。
