Alkaline phosphatase from human uterine myoma. II. Kinetic and immunological properties.

Thermostability of the purified alkaline phosphatase derived from human uterine muscle and myoma was established before and after desialization. Both enzymes were inhibited by sucrose, glucose and maltose in proportion to the carbohydrate concentration. L-Homoarginine inhibits the myoma enzyme in 90%, L-leucine, L-histidine and L-tryptophan in about 60%, and L-phenylalanine in less than 15%. The type of inhibition and Ki values were determined. Muscle and myoma enzymes cross-reacted with antisera against human liver and placental isoenzymes. Molecular and kinetic properties of the enzyme were compared with known human isoenzymes of alkaline phosphatase.