Abstract
Alkaline phosphatases from human adult intestine and fetal intestine (meconium) were purified and compared. Electrophoresis in SDS showed one band of protein in the former. There were three bands of protein in the latter, all with essentially the same peptide map. Thus, two of the bands probably arose by proteolysis of the third, which was largest ( M r 73000). In gradient gels of polyacrylamide the alkaline phosphatase from fetal intestine showed only one band of protein coincident with the band of activity ( M r 151000). Radiolabeled mapping showed that the tryptic peptides of the alkaline phosphatase from fetal intestine were distinctly different from those of adult intestine and human liver, and placenta, indicating a gene distinct from the three that code for the enzyme in liver/kidney/bone, placenta, and adult intestine.
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