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1 Calcium and Reproductive
Biology Laboratory, Department of
Biochemistry, University of Otago,
Dunedin, New Zealand
Biochemical aspects of post-testicular sperm maturation
have been studied. Partial purification of either human
or ram seminal plasma yields a heat-stable, acidic protein which is a Ca2+-dependent regulator of 3':5'-cyclic
nucleotide phosphodiesterase. This protein fraction has
been provisionally named calsemin. Human calsemin
activates the flagellar plasma membrane Ca2+-ATPase
of ram epididymal and ejaculated spermatozoa by 290%
and 20%, respectively. Activation is abolished by trifluoperazine. The addition of calsemin plus Ca2+ to isolated ram caudal spermatozoa results in a three-fold
stimulation of flagellar beat activity. These results lead
us to propose that only after interaction between calsemin and the sperm flagellar plasma membrane can the
Ca2+-ATPase obtain full expression to maximise Ca2+
efflux from the flagellum and thereby cause a stimulation and coordination of sperm flagellar beat activity.
This finding may provide a partial biochemical explanation for the development of mammalian sperm
motility.
Key words: Spermatozoa, initiation of motility, Ca2+-dependent regulator, Ca2+-ATPase, epididymis, seminal plasma
Submitted on August 12, 1981
Revised on November 23, 1981
Accepted on December 3, 1981
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