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Endothelial and bile canalicular alkaline phosphatase in human liver and serum



Endothelial and bile canalicular alkaline phosphatase in human liver and serum



Scandinavian Journal of Clinical and Laboratory Investigation 36(2): 131-135



The alkaline phosphatase in homogenates of human liver was separated into 2 components by the addition of Triton X-100 to an agarose gel electrophoretic system. One of these components migrated at a rate identical to that of the original one and similar to .alpha.2-macroglobulin. The other component migrated more slowly, at a rate that resembled that of .beta.1-transferrin. Human serum samples regularly contained an identical fast-migrating fraction, whereas an identical slowly migrating fraction only appeared in serum obtained from patients with various diseases, especially from patients with malignant tumors, even though the liver did not contain tumor metastases. Slow isoenzyme was found in a few sera that had alkaline phosphatase activity within the normal range. Histochemical examinations of liver tissue from patients whose serum contained the slowly migrating isoenzyme showed a pronounced reaction of alkaline phosphatase in the bile canaliculi, and this isoenzyme seems to arise from the canaliculi. The fast-migrating isoenzyme might arise from the endothelial cells of the liver, to which the activity is usually confined in histochemical stainings.

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Accession: 005359863

Download citation: RISBibTeXText

PMID: 1273491

DOI: 10.1080/00365517609055238



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