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Biology of Reproduction, Vol 3, 327-337, Copyright © 1970 by Society for the Study of Reproduction
1 The Institute for Enzyme Research, University of Wisconsin, Madison 53706 Cytoplasmic droplets have been isolated from bovine epididymal spermatozoa by centrifugation of sperm on a discontinuous sucrose gradient. Once-washed droplets are free
of sperm and essentially free of contaminating soluble and particulate enzymes found in
the medium which had been perfused through the distal caudal epididymis. Examination
of the enzyme content of bovine cytoplasmic droplets indicates that they are rich in hydrolase enzymes which operate over a wide pH range. Droplets contain low activities of
some enzymes linked to the intermediary metabolism of carbohydrates but appear to be
metabolically inert organelles. High levels of hydrolase activity are also found in a particle-free supernatant of the
medium which had been perfused through the epididymis. This fraction contains low levels
of enzymes associated with intermediary metabolism, some of which are not observed in
droplets. A light particulate fraction containing small granules, vesicles, and membrane profiles
has been separated from droplets. This fraction contains hydrolase activity but no enzymes
associated with intermediary metabolism. The presence of a magnesium-dependent nucleotide phosphatase of high specific activity in this fraction differentiates it from droplets and particle-free supernatant. Possible interrelationships and origins of enzyme activities in these fractions are discussed.
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