Abstract
Myometrium obtained from pregnant ewes (30–80 days gestation) contains a factor which inhibits phospholipase A 2 (PLA 2) activity. The activity of this moiety was assessed using an in vitro porcine pancreatic PLA 2 assay system. Inhibitory activity was associated with a 35–45000 dalton molecular weight fraction, heat-labile, sensitive to protease degradation and did not partition into organic solvents. These data are indicative that PLA 2-inhibitory activity resides in a protein moiety. Dixon-plot analysis of myometrial-inhibitory activity was indicative that the inhibition of PLA 2 activity was of a non-competitive nature (K i = 4.1 ± 0.7 μg/ml, ca 118 nmol/1). Myometrial phospholipase-inhibitory protein(s) may be involved in the suppression of eicosanoid biosynthesis by the uterine tissues throughout gestation thus inhibiting uterine contractile activity.
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