[8] Purification and assay of PGH synthase from bovine seminal vesicles

作者: Shozo Yamamoto

DOI: 10.1016/0076-6879(82)86168-5

关键词:

摘要: Publisher Summary This chapter presents a procedure for the purification and assay of prostaglandin H (PGH) synthase from bovine seminal vesicles. An enzyme preparation PGH purified to an apparent homogeneity microsomes vesicle catalyzes two reactions. One is fatty acid cyclooxygenase reaction producing G 2 (PGG ) arachidonic acid. bisdioxygenase incorporating molecules oxygen into The other hydroperoxidase in which 15-hydroperoxide PGG converted hydroxyl group produce . These activities have not been resolved various experimental conditions, results suggesting that either separate are attributed one protein or proteins tightly bound. Thus, with referred as PG endoperoxide synthetase synthase. Two assays provided quantitation: assay.

参考文章(4)
S. Ohki, N. Ogino, S. Yamamoto, O. Hayaishi, Prostaglandin hydroperoxidase, an integral part of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes. Journal of Biological Chemistry. ,vol. 254, pp. 829- 836 ,(1979) , 10.1016/S0021-9258(17)37880-8
T Miyamoto, N Ogino, S Yamamoto, O Hayaishi, Purification of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes. Journal of Biological Chemistry. ,vol. 251, pp. 2629- 2636 ,(1976) , 10.1016/S0021-9258(17)33534-2
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)