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. 1990 Jul;10:6–11.

Purification and characterisation of the placental-like alkaline phosphatase from ovarian epithelial tumours.

I Koyama 1, K Hirano 1, R Makiya 1, U Stendahl 1, T Stigbrand 1
PMCID: PMC2149509  PMID: 2383481

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Beckman L., Björling G., Christodoulou C. Pregnancy enzymes and placental polymorphism. I. Alkaline phosphatse. Acta Genet Stat Med. 1966;16(1):59–73. doi: 10.1159/000151950. [DOI] [PubMed] [Google Scholar]
  2. Berger J., Garattini E., Hua J. C., Udenfriend S. Cloning and sequencing of human intestinal alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1987 Feb;84(3):695–698. doi: 10.1073/pnas.84.3.695. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Birkett D. J., Conyers R. A., Neale F. C., Posen S., Brudenell-Woods J. Action of urea on human alkaline phosphatases: with a description of some automated techniques for the study of enzyme kinetics. Arch Biochem Biophys. 1967 Aug;121(2):470–479. doi: 10.1016/0003-9861(67)90102-6. [DOI] [PubMed] [Google Scholar]
  4. Conyers R. A., Birkett D. J., Neale F. C., Posen S., Brudenell-Woods J. The action of EDTA on human alkaline phosphatases. Biochim Biophys Acta. 1967 Jul 11;139(2):363–371. doi: 10.1016/0005-2744(67)90040-x. [DOI] [PubMed] [Google Scholar]
  5. Cox R. P., Elson N. A., Tu S. H., Griffin M. J. Hormonal induction of alkaline phosphatase activity by an increase in catalytic efficiency of the enzyme. J Mol Biol. 1971 May 28;58(1):197–215. doi: 10.1016/0022-2836(71)90241-5. [DOI] [PubMed] [Google Scholar]
  6. Endo T., Ohbayashi H., Hayashi Y., Ikehara Y., Kochibe N., Kobata A. Structural study on the carbohydrate moiety of human placental alkaline phosphatase. J Biochem. 1988 Jan;103(1):182–187. doi: 10.1093/oxfordjournals.jbchem.a122228. [DOI] [PubMed] [Google Scholar]
  7. Fishman W. H. Oncotrophoblast gene expression: placental alkaline phosphatase. Adv Cancer Res. 1987;48:1–35. doi: 10.1016/s0065-230x(08)60689-2. [DOI] [PubMed] [Google Scholar]
  8. Haije W. G., van Driel J., van der Burg M. E. Catalytic and immunologic activities of placental-like alkaline phosphatase in clinical studies. The value of PLAP in follow-up of ovarian cancer. Clin Chim Acta. 1987 Jun 15;165(2-3):165–175. doi: 10.1016/0009-8981(87)90160-4. [DOI] [PubMed] [Google Scholar]
  9. Henthorn P. S., Knoll B. J., Raducha M., Rothblum K. N., Slaughter C., Weiss M., Lafferty M. A., Fischer T., Harris H. Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids. Proc Natl Acad Sci U S A. 1986 Aug;83(15):5597–5601. doi: 10.1073/pnas.83.15.5597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hirano K., Iiizumi Y., Hayashi Y., Tanaka T., Sugiura M., Hayashi K., Lu Z. D., Iino S. A highly sensitive assay method for human placental alkaline phosphatase involving a monoclonal antibody bound to a paper disk. Anal Biochem. 1986 May 1;154(2):624–631. doi: 10.1016/0003-2697(86)90038-2. [DOI] [PubMed] [Google Scholar]
  11. Hirano K., Matsumoto H., Tanaka T., Hayashi Y., Iino S., Domar U., Stigbrand T. Specific assays for human alkaline phosphatase isozymes. Clin Chim Acta. 1987 Jul 15;166(2-3):265–273. doi: 10.1016/0009-8981(87)90429-3. [DOI] [PubMed] [Google Scholar]
  12. Jemmerson R., Millan J. L., Klier F. G., Fishman W. H. Monoclonal antibodies block the bromelain-mediated release of human placental alkaline phosphatase from cultured cancer cells. FEBS Lett. 1985 Jan 7;179(2):316–320. doi: 10.1016/0014-5793(85)80542-1. [DOI] [PubMed] [Google Scholar]
  13. Jemmerson R., Stigbrand T. Monoclonal antibodies block the trypsin cleavage site on human placental alkaline phosphatase. FEBS Lett. 1984 Aug 6;173(2):357–359. doi: 10.1016/0014-5793(84)80805-4. [DOI] [PubMed] [Google Scholar]
  14. Jeppsson A., Wahren B., Brehmer-Andersson E., Silfverswärd C., Stigbrand T., Millán J. L. Eutopic expression of placental-like alkaline phosphatase in testicular tumors. Int J Cancer. 1984 Dec 15;34(6):757–761. doi: 10.1002/ijc.2910340604. [DOI] [PubMed] [Google Scholar]
  15. Kam W., Clauser E., Kim Y. S., Kan Y. W., Rutter W. J. Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8715–8719. doi: 10.1073/pnas.82.24.8715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Koyama I., Arai Y., Miura M., Matsuzaki H., Sakagishi Y., Komoda T. Similarity of the sugar moiety of human alkaline phosphatases between the kidney cortex and duodenum, or medulla and ileum. Clin Chim Acta. 1988 Apr 15;173(2):139–146. doi: 10.1016/0009-8981(88)90251-3. [DOI] [PubMed] [Google Scholar]
  17. Koyama I., Komoda T., Sakagishi Y., Kurata M. A possible mechanism for the changes in hepatic and intestinal alkaline phosphatase activities in bile-duct-ligated rats or guinea pigs. Biochim Biophys Acta. 1983 Oct 4;760(1):169–174. doi: 10.1016/0304-4165(83)90139-3. [DOI] [PubMed] [Google Scholar]
  18. Koyama I., Miura M., Matsuzaki H., Sakagishi Y., Komoda T. Sugar-chain heterogeneity of human alkaline phosphatases: differences between normal and tumour-associated isozymes. J Chromatogr. 1987 Jan 23;413:65–78. doi: 10.1016/0378-4347(87)80214-1. [DOI] [PubMed] [Google Scholar]
  19. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  20. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  21. Mano H., Furuhashi Y., Morikawa Y., Hattori S. E., Goto S., Tomoda Y. Radioimmunoassay of placental alkaline phosphatase in ovarian cancer sera and tissues. Obstet Gynecol. 1986 Dec;68(6):759–764. [PubMed] [Google Scholar]
  22. Millán J. L., Manes T. Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc Natl Acad Sci U S A. 1988 May;85(9):3024–3028. doi: 10.1073/pnas.85.9.3024. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Millán J. L. Molecular cloning and sequence analysis of human placental alkaline phosphatase. J Biol Chem. 1986 Mar 5;261(7):3112–3115. [PubMed] [Google Scholar]
  24. Nakayama T., Kitamura M. L-leucine sensitive alkaline phosphatase isozyme from cancer tissue. Ann N Y Acad Sci. 1975 Aug 22;259:325–336. doi: 10.1111/j.1749-6632.1975.tb25429.x. [DOI] [PubMed] [Google Scholar]
  25. Ogata S. I., Muramatsu T., Kobata A. New structural characteristic of the large glycopeptides from transformed cells. Nature. 1976 Feb 19;259(5544):580–582. doi: 10.1038/259580a0. [DOI] [PubMed] [Google Scholar]
  26. Ogata S., Hayashi Y., Takami N., Ikehara Y. Chemical characterization of the membrane-anchoring domain of human placental alkaline phosphatase. J Biol Chem. 1988 Jul 25;263(21):10489–10494. [PubMed] [Google Scholar]
  27. Seiffert U. B., Siede W. H., Welsch G. J., Oremek G. Multiple forms of alkaline phosphatases in human liver tissue. Clin Chim Acta. 1984 Dec 15;144(1):17–27. doi: 10.1016/0009-8981(84)90256-0. [DOI] [PubMed] [Google Scholar]
  28. Taylor D. D., Homesley H. D., Doellgast G. J. Binding of specific peroxidase-labeled antibody to placental-type phosphatase on tumor-derived membrane fragments. Cancer Res. 1980 Nov;40(11):4064–4069. [PubMed] [Google Scholar]
  29. Weiss M. J., Henthorn P. S., Lafferty M. A., Slaughter C., Raducha M., Harris H. Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7182–7186. doi: 10.1073/pnas.83.19.7182. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Yamashita K., Hitoi A., Taniguchi N., Yokosawa N., Tsukada Y., Kobata A. Comparative study of the sugar chains of gamma-glutamyltranspeptidases purified from rat liver and rat AH-66 hepatoma cells. Cancer Res. 1983 Nov;43(11):5059–5063. [PubMed] [Google Scholar]
  31. Yoshima H., Mizuochi T., Ishii M., Kobata A. Structure of the asparagine-linked sugar chains of alpha-fetoprotein purified from human ascites fluid. Cancer Res. 1980 Nov;40(11):4276–4281. [PubMed] [Google Scholar]

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