We have reported that the electrophoretic mobility of human intestinal alkaline phosphatase (ALP) was different from that of adult intestinal ALP, and meconium ALP had the same enzymatic properties and electrophoretic mobilities as that of fetal intestinal ALP. In this report, using meconium ALP instead of fetal intestinal ALP, their properties were compared with that of the purified human intestinal ALP.
The results obtained were as follows:
1) The electrophoretic mobilities of meconium ALP were different from that of adult intestinal ALP.
2) The electrophoretic mobilities of a new-born baby's fecal ALP moved gradually to the cathode after birth. On the 5th day after birth, its mobility became similar to that of adult intestinal ALP.
3) On enzymatic properties, such as heat-stability, Km value and effects of many inhibitors, meconium ALP and adult intestinal ALP were similar.
4) By double immunodiffusion and electrophoresis with human anti-intestinal ALP antibody, they showed identical reaction.
5) By neuraminidase treatment, meconium ALP migrated to the cathode and the same position as adult intestinal ALP which showed no migration by this treatment.
6) These results showed that fetal intestinal ALP is not the new ALP isoenzyme but is the modified enzyme of adult intestinal ALP. The difference in their electrophoretic mobilities is probably determined by the amount of sialic acids contained in this enzyme.
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