Am. Brown et al., MOLECULAR ACTIVATION DEACTIVATION OF XANTHINE-OXIDASE IN HUMAN-MILK, Biochimica et biophysica acta (G). General subjects, 1245(2), 1995, pp. 248-254
Enzymic activity and protein levels of xanthine oxidase were measured
in serial samples of breast milk donated by each of 14 mothers, starti
ng, in all but two cases, within 7 days following parturition. Enzyme
activity varied widely, usually reaching peak values during the first
15 days and falling thereafter, by as much as 98%, to basal levels tha
t were subsequently largely maintained. Corresponding changes in xanth
ine oxidase protein levels were not observed and, consequently, the sp
ecific activity of xanthine oxidase followed the above pattern. The ca
pacity of human xanthine oxidase to undergo activation-deactivation cy
cles at the molecular level has important implications, not only for i
ts role in breast milk, but also for its potential as a source of reac
tive oxygen species in other human tissues.