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The development of a method to measure small amounts of nucleotides would be of considerable value in experiments concerned with metabolism in mammalian spermatozoa. As the adenine nucleotides have been shown to be the predominant nucleotides in mammalian spermatozoa (Brooks, 1970), measurement of ATP and ADP by the luciferin-luciferase system appeared to be a method ideally suited to this purpose. Ejaculated bull semen, collected by artificial vagina, was used in the present work. The measurement of ATP was carried out in a Packard Model 3380 liquid scintillation spectrometer calibrated according to Stanley & Williams (1969). The phosphate buffer described by these workers was altered to include 2 mm-EDTA and 2 mm-2-mercaptoethanol. In addition, the luciferin\x=req-\ luciferase preparation made up in arsenate buffer was incubated with apyrase to reduce background luminescence (Lyman & DeVincenzo, 1967). ADP was measured as the increase in luminescence after conversion to ATP (Holmsen, Holmsen & Bernhardsen, 1966). The conversion was achieved by incubating sample aliquots in vials in which the phosphate buffer contained 2 \g=m\leach of pyruvate kinase suspension (The Boehringer Corporation) and 10 mm-phosphoenolpyruvate. The conversion was complete in 10 min at room temperature, and finally the enzyme was inhibited by addition of the arsenate buffer. Preliminary experiments were carried out to compare two methods of nucleotide extraction as applicable to small samples (1 ml) of semen. (i) The semen was added directly to 1 ml of ice-cold 20% trichloroacetic acid (TCA) in

OBSERVATIONS ON THE CONTENT OF ATP AND ADP IN BULL SPERMATOZOA USING THE FIREFLY LUCIFERASE SYSTEM