Mammalian serum and plasma contain an endogenous inhibitor of prostaglandin synthetase (EIPS). Human plasma fractions rich in EIPS show anti-inflammatory activity in vivo. In rats, glucocorticoids raise EIPS activity of plasma and serum. These findings suggest the existence of a natural mechanism of controlling prostaglandin synthesis, possibly related to corticosteroid action.

No abstract

Seven peroxidase isoenzymes were purified from crude horseradish peroxidase (EC 1.11.1.7) (HRP) in a single step by preparative polyacrylamide gel electrophoresis. The peroxidase activity in seven isoenzymes accounted for 90% of the activity in the crude material. Each isoenzyme (except HRP7) after separation migrated as a single band with characteristic electrophoretic mobility. All of the purified isoenzymes were found to retain complete peroxidase activity after storage at −20 °C or 4 °C for 3 months.