Research Article| Volume 6, ISSUE 3, P507-523, September 1986

Electrophoresis of Human Alkaline and Acid Phosphatases

  • Donald W. Moss
    Corresponding Author: Hammersmith Hospital, Ducane Road, London W12 OHS, United Kingdom.
    Professor of Clinical Enzymology, Royal Postgraduate Medical School (University of London), and Honorary Biochemist, Hammersmith Hospital, London, United Kingdom
    Search for articles by this author
      This paper is only available as a PDF. To read, Please Download here.
      Zone electrophoresis has played an important part in understanding the inter- and intratissue heterogeneity of acid and alkaline phosphatases. Electrophoresis of alkaline phosphatase in serum is of practical diagnostic value in deciding between liver and bone as alternative, or coexisting, sources of a raised total activity and, more rarely, in helping to define the contributions of other alkaline phosphatase isoenzymes. Certain tissue-specific patterns of acid phosphatase zones are also diagnostically useful in confirming the identity of isoenzymes in serum indicated by other techniques.
      To read this article in full you will need to make a payment

      Purchase one-time access:

      Academic & Personal: 24 hour online accessCorporate R&D Professionals: 24 hour online access
      One-time access price info
      • For academic or personal research use, select 'Academic and Personal'
      • For corporate R&D use, select 'Corporate R&D Professionals'

      Subscribers receive full online access to your subscription and archive of back issues up to and including 2002.

      Content published before 2002 is available via pay-per-view purchase only.


      Subscribe to Clinics in Laboratory Medicine
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Institutional Access: Sign in to ScienceDirect


        • Axline S.G.
        Isozymes of acid phosphatase in normal and Calmette-Guerin bacillus induced rabbit alveolar macrophages.
        J. Exp. Med. 1968; 128: 1031-1048
        • Brock D.J.H.
        • Bedgood D.
        • Barron L.
        • Hayward C.
        Prospective prenatal diagnosis of cystic fibrosis.
        Lancet. 1985; 1: 1175-1178
        • Brocklehurst D.
        • Wilde C.E.
        • Doar J.W.H.
        The incidence and likely origins of serum particulate alkaline phosphatase and lipoprotein-X in liver disease.
        Clin. Chim. Acta. 1978; 88: 509-515
      1. Bücher, T., Dünnwald, M., Führer, F., et al.: Quantitative evaluation of serum alkaline phosphatase isoenzyme patterns (abstract). Joint Meeting, Belgian, Dutch, German, and British Societies for Clin. Chem., Newcastle-on-Tyne, U.K., May 1983.

        • Crofton P.M.
        • Smith A.F.
        High-molecular-mass alkaline phosphatase in serum and bile. Nature and relationship with lipoprotein-X.
        Clin. Chem. 1981; 27: 867-874
        • DeBroe M.E.
        • Borgers M.
        • Wieme R.J.
        The separation and characterization of liver plasma membrane fragments circulating in the blood of patients with cholestasis.
        Clin. Chim. Acta. 1975; 59: 369-372
        • DeBroe M.E.
        • Mets T.E.
        • Loroux-Roels G.G.
        • et al.
        Occurrence of immunoglobulin G-alkaline phosphatase complexes in human serum.
        Ann. Intern. Med. 1979; 90: 30-35
        • Dent C.E.
        • Norris T.S.M.
        • Smith R.
        • et al.
        Steatorrhea with striking increase of plasma alkaline phosphatase of intestinal origin.
        Lancet. 1968; 1: 1333-1336
        • Donald L.J.
        • Robson E.B.
        Rare variants of placental alkaline phosphatase.
        Ann. Hum. Genet. 1974; 37: 303-313
        • Efstratiadis T.
        • Moss D.W.
        Tartrate-resistant acid phosphatase of human lung. Apparant identity with osteoclastic acid phosphatase.
        Enzyme. 1985; 33: 34-40
        • Efstratiadis T.
        • Moss D.W.
        Tartrate-resistant acid phosphatase in human alveolar macrophages.
        Enzyme. 1985; 34: 140-143
        • Epstein E.
        • Baginski E.S.
        • Zak B.
        Detergent altered alkaline phosphatase patterns of liver disease.
        Ann. Clin. Lab. Sci. 1978; 3: 34-41
        • Epstein E.
        • Wolf P.L.
        • Horowitz J.P.
        • et al.
        An indigogenic reaction for alkaline phosphatase in disk electrophoresis.
        Tech. Bull. R.M.T. 1967; 37: 530-534
        • Fishman L.
        Acrylamide disc gel electrophoresis of alkaline phosphatase of human tissues, serum and ascites fluid using Triton X-100 in the sample and gel matrix.
        Biochem. Med. 1974; 9: 309-315
        • Fritsche Jr., H.A.
        • Adams-Park H.R.
        Cellulose acetate electrophoresis of alkaline phosphatase isoenzymes in human serum and tissue.
        Clin. Chem. 1972; 13: 417-421
        • Hagerstrand I.
        • Skude G.
        Improved electrophoretic resolution of human serum alkaline phosphatase isoenzymes in agarose gel by Triton X-100.
        Scand. J. Clin. Lab. Invest. 1976; 36: 127-129
        • Haije W.G.
        • Dejong M.
        Iso-enzyme patterns of serum alkaline phosphatase in agar-gel electrophoresis and their clinical significance.
        Clin. Chim. Acta. 1963; 3: 620-623
        • Higashino K.
        • Otani R.
        • Kudo S.
        • et al.
        A fetal intestinal-type alkaline phosphatase in hepatocellular carcinoma tissue, Clin.
        Chem. 1977; 23: 1615-1623
        • Hill P.G.
        • Sammons H.G.
        An interpretation of the elevation of serum alkaline phosphatase in disease.
        J. Clin. Pathol. 1967; 20: 654-659
        • Hodson A.W.
        • Latner A.L.
        • Raine L.
        Iso-enzymes of alkaline phosphatase.
        Clin. Chim. Acta. 1962; 7: 255-261
        • Hopkinson D.A.
        • Spencer N.
        • Harris H.
        Red-cell acid phosphatase variants. A new human polymorphism.
        Nature (London). 1963; 199: 969-971
        • Kowlessar O.D.
        • Pert J.H.
        • Haeffner L.J.
        • Sliesenger M.H.
        Localization of 5-nucleotidase and non-specific alkaline phosphatase by starch gel electrophoresis.
        Proc. Soc. Exp. Biol. Med. 1959; 100: 191-193
        • Lam W.K.W.
        • Lai L.C.
        • Yam L.T.
        Tartrate-resistant (band 5) acid phosphatase activity measured by electrophoresis on acrylamide gel.
        Clin. Chem. 1978; 24: 309-312
        • Langman M.J.S.
        • Leuthold E.
        • Robson E.B.
        • et al.
        Influence of diet on the intestinal component of serum alkaline phosphatase in people of different ABO blood groups and secretor-status.
        Nature (London). 1966; 212: 41-43
        • Latner A.L.
        Phosphatase isoenzymes.
        in: Ruyssen R. Vanderdriessche L. Enzymes in Clinical Chemistry. Elsevier, Amsterdam1963: 110-118
        • Li C.Y.
        • Yam L.T.
        • Lam K.W.
        Studies of acid phosphatase isoenzymes in human leukocytes. Demonstration of isoenzyme cell specificity.
        J. Histochem. Cytochem. 1970; 18: 901-910
        • McKenna M.J.
        • Hamilton T.A.
        • Sussman H.H.
        Comparison of human alkaline phosphatase isoenzymes. Structural evidence for three protein classes.
        Biochem. J. 1979; 81: 67-73
        • Miki K.
        • Suzuki H.
        • Iino S.
        • et al.
        Human fetal intestinal alkaline phosphatase.
        Clin Chim. Acta. 1977; 79: 21-30
        • Moss D.W.
        Chemical modification of alkaline phosphatases. The effects of amino-group reagents on the electrophoretic mobilities and activities of phosphatases from several human tissues.
        Enzymologia. 1970; 39: 319-330
        • Moss D.W.
        Alkaline phosphatase isoenzymes: Technical and clinical aspects.
        Enzyme. 1975; 20: 20-34
        • Moss D.W.
        Alkaline phosphatase isoenzymes.
        Clin. Chem. 1982; 28: 2007-2016
        • Moss D.W.
        Acid phosphatase: An archetype of the role of isoenzyme analysis in clinical enzymology.
        in: Goldberg D.M. Werner M. Progress in Clinical Enzymology-2. Masson, New York1983: 113-123
        • Moss D.W.
        • Campbell D.M.
        • Anagnostou-Kakaras E.
        • et al.
        Characterization of tissue alkaline phosphatases and their partial purification by starch-gel electrophoresis.
        Biochem. J. 1961; 81: 441-447
        • Moss D.W.
        • Edwards R.K.
        Improved electrophoretic resolution of bone and liver alkaline phosphatases resulting from partial digestion with neuraminidase.
        Clin. Chim. Acta. 1984; 143: 177-182
      2. Moss, D. W., and Efstratiadis, T.: The selective expression of human acid phosphate isoenzymes. In Goldberg, D. M., Werner, E., and de la Morena, E. (eds): Advances in Clinical Enzymology. Volume 4. Basel, Karger, in press.

        • Moss D.W.
        • Thomas D.M.
        Modification of the electrophoretic mobility of serum alkaline phosphatase by acetylation.
        Clin. Chim. Acta. 1970; 30: 835-838
        • Moss D.W.
        • Whitby L.G.
        A simplified heat-inactivation method for investigating alkaline phosphatase isoenzymes in serum.
        Clin. Chim. Acta. 1975; 61: 63-71
        • Nagamine M.
        • Okhuma S.
        Serum alkaline phosphatase isoenzymes linked to immunoglobulin G.
        Clin. Chim. Acta. 1975; 65: 39-46
        • Newton M.A.
        The clinical application of alkaline phosphatase electrophoresis.
        Q. J. Med. 1967; 36: 17-28
        • Price C.P.
        • Sammons H.G.
        The nature of the serum alkaline phosphatases in liver diseases.
        J. Clin. Pathol. 1974; 27: 392-398
        • Rosalki S.B.
        • Foo A.Y.
        Two new methods for separating and quantifying bone and liver alkaline phosphatase isoenzymes in plasma.
        Clin. Chem. 1984; 30: 1182-1186
        • Smith I.
        • Lightstone P.J.
        • Perry J.D.
        Separation of human alkaline phosphatases by electrophoresis on acrylamide disc gels.
        Clin. Chim. Acta. 1968; 19: 499-505
        • Smith J.K.
        • Whitby L.G.
        The heterogeneity of prostatic acid phosphatase.
        Biochim. Biophys. Acta. 1968; 151: 607-618
        • Stigbrand T.
        • Fishman W.H.
        Human Alkaline Phosphatases.
        A. R. Liss, New York1984
        • Stinson R.A.
        • Seargeant L.E.
        Comparative studies of pure alkaline phosphatases from five human tissues.
        Clin. Chim. Acta. 1981; 110: 261-272
        • Stolbach L.L.
        • Krant M.J.
        • Inglis N.R.
        • et al.
        Correlation of serum L-phenylalanine sensitive alkaline phosphatase derived from intestine with ABO blood group of cirrhotics.
        Gastroenterology. 1967; 52: 819-827
        • Sur B.K.
        • Moss D.W.
        • King E.J.
        Starch-gel electrophoresis of prostatic acid phosphatase.
        Proc. Assoc. Clin. Biochemists. 1962; 2: 11-13
        • Taswell H.F.
        • Jeffers D.M.
        Isoenzymes of alkaline phosphatase in hepatobiliary and skeletal disease.
        Am. J. Clin. Pathol. 1963; 40: 349-356
        • Van Belle H.
        Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans.
        Clin. Chem. 1976; 22: 972-976
        • Walker A.W.
        Intestinal alkaline phosphatase in serum of patients on maintenance haemodialysis.
        Clin. Chim. Acta. 1974; 55: 399-405
        • Warnock M.L.
        • Reisman R.
        Variant alkaline phosphatase in human hepatocellular cancers.
        Clin. Chim. Acta. 1969; 24: 5-11
        • Watanabe F.
        • Takano M.
        • Tanaka F.
        • et al.
        The analysis of alkaline phosphatase isoenzyme using 4-methylumbelliferyl phosphate as substrate on a cellulose acetate membrane.
        Clin. Chim. Acta. 1979; 91: 273-276
        • Whitaker K.B.
        • Eckland S.
        • Hodgson H.J.F.
        • et al.
        A variant alkaline phosphatase in renal cell carcinoma.
        Clin. Chem. 1982; 28: 374-377
        • Whitaker K.B.
        • Whitby L.G.
        • Moss D.W.
        Quantitative determination of activities of alkaline phosphatase isoenzymes in serum.
        in: Goldberg D.M. Wilkinson J.H. Enzymes in Health and Disease. Karger, Basel1978: 127-130