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Cholesterol and phospholipid concentrations and phospholipase activity were measured in fluid from cannulae collected from the bovine oviductal isthmus and ampulla at different stages of the oestrous cycle. The cholesterol concentration and cholesterol normalized by protein were significantly (P = 0.03) greater in isthmic oviductal fluid (224.3 ± 42.7 μg ml⁻¹ over all stages) than in ampullary oviductal fluid (164.5 ± 11.3 μg ml⁻¹), and maximal concentrations (284.5 ± 25.5 μg ml⁻¹) were found during the luteal stage (serum progesterone concentration ≥ 1.5 ng ml⁻¹). The concentrations of the phospholipids sphingomyelin and lysophosphatidylcholine increased at different stages of the cycle and in different regions. In the ampulla, the concentration of sphingomyelin was significantly (P < 0.05) greater in oviductal fluid collected during the luteal phase (12.1 ± 2.7% of total phospholipids) than in fluid collected near oestrus and ovulation (7.5 ± 1.5% and 6.9 ± 1%, respectively). The concentration of lysophosphatidylcholine was greater (P < 0.01) in ampullary (19.2 ± 1.6% of total phospholipids) than in isthmic oviductal fluid (9.9 ± 1.1%) collected near ovulation. The ratio of cholesterol to total phospholipid was highest in oviductal fluid collected from the isthmus during all stages (2.3 μg ml⁻¹:% total phospholipid), while the minimal ratio was found in ampullary fluid collected near ovulation (1.5). Phospholipase activity was higher (P = 0.03) in isthmic oviductal fluid (20.4 ± 3.2% product formed) than in ampullary oviductal fluid (14.6 ± 1.4%); the lowest activity (12.6 ± 1.7% product formed) was in fluid collected during the phase of the oestrous cycle immediately before ovulation. We conclude that the regional and temporal differences in the concentrations of lipids in oviductal fluid provide general support for the concept that the isthmus serves as a sperm reservoir, while the ampulla is the site of the bovine sperm acrosome reaction.

Summary. After extra-amniotic treatment of pregnant rhesus monkeys premature parturition was induced in 4 given 2·5 mg PGE-2; none of the 4 monkeys given 100 mg arachidonic acid were affected. The concentrations of PGE, PGF or 13,14-dihydro-15-oxo-PGF did not change after arachidonic acid treatment, but all increased after PGE-2. It is suggested that the availability of substrate, arachidonic acid, is not a major factor governing the control of PG synthesis but that the latter is suppressed during pregnancy.

Summary. Human placental protein 14 (PP14) has been purified in high yield from first trimester decidual cytosol. High-performance liquid chromatography on anion exchange, gel filtration and reverse-phase chromatography were used. The protein obtained is approximately 97% pure with an overall recovery of about 50% from the original tissue extract. The first 24 amino acids of the N-terminal were found to be Met-Asp-Ile-Pro-Gln-Thr-Lys-Gln-Asp-Leu-Glu-Leu-Pro-Lys-Leu-Ala-Gly-Thr-Glu-His-Glu-Met-Ala-Met. PP14 has been characterized in this study to be a dimeric glycoprotein of M _r 60 000, with homologous subunits having an M _r of 28 000.

Keywords: human; PP14; decidual cytosol; h.p.l.c. techniques