THE INTRINSIC MECHANISM OF CHROMATIN DECONDENSATION AND ITS ACTIVATION IN HUMAN SPERMATOZOA

In vitro decondensation of human sperm chromatin induced by the activation of an intrinsic mechanism was studied by light microscopy, scanning and transmission electron microscopy. Morphological evidence was provided to support the concept that this mechanism is essential for the chromatin decondensation occurring in vivo. Prostatic zinc is hypothesized to preserve this potential decondensation ability from oxidative destruction, by reversibly binding to free thiol-groups. The unique occurrence of disulphide-stabilized structures in eutherian spermatozoa may serve to protect the spermatozoon from structural degradation by its own proteolytic activity during the relatively slow passage through the eutherian egg investments.