Fetal forms of oligoaminopeptidase, dipeptidylaminopeptidase IV, and sucrase in human intestine and meconium.

Particles of meconium sedimenting at 105,000 g contain sucrase and various brush border peptidase activities. Oligoaminopeptidase, dipeptidylaminopeptidase, and sucrase solubilized by papain from meconium particles of preterm newborns or from brush border of human fetuses during the 4th month of gestation were compared with the same enzymes prepared from adult jejunal and ileal brush border. The following are characteristics of fetal intestinal brush border enzymes: (a) a faster anodal electrophoretic mobility in polyacrylamide and in agar gel; (b) the same specific activity, as measured by quantitative crossed immunoelectrophoresis utilizing an antiserum against adult brush border membranes; (c) complete fusion of the immunoprecipitation lines with the adult enzymes by using the same antiserum; and (d) a different binding pattern to Helix pomatia lectin and lentil lectin. The results suggest that the charge difference between adult and fetal human brush border enzymes, which causes the difference in the gel electrophoretic mobility, is most probably due, at least in part, to differences in carbohydrate composition of these glycoproteins. Extensive neuraminidase digestion causes no or only minor changes of the electrophoretic mobility of the meconial enzymes. The difference between adult and meconial enzymes is therefore apparently not, or not only, due to different sialic acid content. These results suggest that many intestinal brush border enzymes in fetal life and at birth are in forms structurally different from those in adult life.