Protease Inhibitors in Human Milk

Publisher Website
Google Scholar
Abstract
Summary: Protease inhibitors (inhibiting trypsin, chymotrypsin, and elastase) were demonstrated in human milk from birth to 4 months after delivery. No pepsin inhibitor was found. The protease inhibitors were localized in the α1-region—inhibiting trypsin, chymotrypsin, and elastase—and in a more cathodal region—inhibiting chymotrypsin—in agarose gel electrophoresis of human milk. α1-antitrypsin and antichymotrypsin were demonstrated by crossed immunoelectrophoresis. Electroimmunoassay showed the concentration of α1-antitrypsin in 1st day milk to be 10.9% and the concentration of antichymotrypsin was 116% of that of adult serum. The concentrations decreased during the 1st wk; from 1 wk to 4 months they were 1.6% for α1-antitrypsin and 3.8% for antichymotrypsin of those of adult serum. One ml of human milk from the first 3 days inhibits, by enzymatic methods, 0–150 μg (mean value, 70 μg) trypsin. Milk from 1 week after delivery and later inhibits 0–65 μg (mean value, 38 μg) trypsin per ml. Speculation: Protease inhibitors are present in large amounts in, for example, bovine and porcine colostrum and play a role in the intestinal absorption of proteins, i.e., immunoglobulins, in the newborn animal. Although the concentration of protease inhibitors in human milk is much lower, they might play a role in the local immunity in the lumen of the gut and in the enhanced absorption of proteins occurring in early infancy.