Purification and characterisation of the placental-like alkaline phosphatase from ovarian epithelial tumours.
The placental alkaline phosphatase was purified by immunoaffinity chromatography from ovarian epithelial tumours to homogeneity. Up to 40% of the catalytical phosphatase activity in these tumours was derived from this placental type alkaline phosphatase (PLAP). The purified enzyme were similar to those of PLAP, whereas the PLAP-like isozyme was more heat-stable and resistant to 8 M urea than PLAP. The amino terminal sequence of the PLAP-like enzyme demonstrated heterogeneity at position three in the N-terminal end compared with PLAP. Phenyl-Sepharose affinity chromatography and different lectin chromatographies demonstrated the tumour-derived enzyme to be microheterogeneous, both with regard to concanavalin A binding and hydrophobicity properties.
Koyama
I
I
Department of Physiological Chemistry, University of Umeå, Sweden.
Hirano
K
K
Makiya
R
R
Stendahl
U
U
Stigbrand
T
T
D000469:Alkaline Phosphatase / Q000302:isolation & purification* / Q000378:metabolism; D014408:Biomarkers, Tumor; D002846:Chromatography, Affinity; D003208:Concanavalin A / Q000378:metabolism; D003537:Cystadenoma / Q000201:enzymology*; D004586:Electrophoresis; D005260:Female; D058851:GPI-Linked Proteins; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D010051:Ovarian Neoplasms / Q000201:enzymology*
D014408:Biomarkers, Tumor; D058851:GPI-Linked Proteins; D007527:Isoenzymes; C055791:germ-cell AP isoenzyme; D003208:Concanavalin A; D000469:Alkaline Phosphatase; C019839:alkaline phosphatase, placental