Acrolysin,the aminoproteinase catalyzing the initial conversion of proacrosin to acrosin in mammalian fertilization

Extracts of mammalian sperm acrosomes and testes contain a proteinase, acrolysin, that hydrolyzes the aminopeptide bonds of hydrophobic aminoacyl residues. Acrolysin has hydrolytic specificity and properties similar to the proteinase, thermolysin (E.C. 3.4.24.4), that also catalyzes the conversion of proacrosin to acrosin (E.C. 3.4.21.10). Acrolysin is the apparent initiator of proacrosin activation in mammalian fertilization.     

Maternal and paternal periods in the development of infant Callimico goeldii

The paternal-maternal-infant interactions of contact and nursing are reported from extensive longitudinal observations on two successive Callimico births in one family. For the first two weeks, the maternal period, the infant clings exclusively to the female. In the third week the infant shifts abruptly to the male. Subsequently, during the paternal period most of the maternal-infant contact involves nursing. The infant Callimico remains almost totally dependent until week 6, but even in week 11 it spends less than 50% of the time off a parent.