Skip to main content
SpringerLink
Log in

Studies of rat alkaline phosphatase

I. Development of methods for detecting isoenzymes

  • Original Investigations
  • Published:
Archives of Toxicology Aims and scope Submit manuscript

Abstract

A manual system of various estimations of rat plasma alkaline phosphatase activity has been devised for small volumes of plasma which uses different inhibitors, compares the utilisation of two substrates and includes acrylamide gel electrophoresis. The different inhibitors etc. allow a degree of discrimination between alkaline phosphatase extracts of rat organs. The properties of isoenzymes, e.g. intestinal alkaline phosphatase, differ depending upon the environment in which they are studied. In conjunction, if necessary, with the methods described for the estimation of liver and intestinal alkaline phosphatase activity, it is hoped to use the system to discriminate between the isoenzymes present in the plasma alkaline phosphatase of rats in toxicological studies.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Ashton, G. C., Braden, A. W. H.: Serum β-globulin polymorphism in mice. Aust. J. biol. Sci. 14, 248–253 (1961)

    Google Scholar 

  • Bates, R. G., Pinching, G. D., Smith, E. R.: pH standards of high acidity and high alkalinity and the practical scale of pH. J. Research NBS 45, 418–429 (1950)

    Google Scholar 

  • Belfield, A., Goldberg, D. M.: Revised assay for serum phenyl phosphatase activity using 4-amino-antipyrine. Enzyme 12, 561–573 (1971)

    Google Scholar 

  • Boyer, S. H., Fainer, D. C., Naughton, M. A.: Myoglobin: Inherited structural variation in man. Science 140, 1228–1231 (1963)

    Google Scholar 

  • Ferguson, K. A., Wallace, A. L. C.: Starch-gel electrophoresis of anterior pituitary hormones. Nature (Lond.) 190, 629–630 (1961)

    Google Scholar 

  • Fishman, W. H., Sie, H. G.: l-Homoarginine: an inhibitor of serum bone and liver alkaline phosphatase. Clin. chim. Acta 29, 339–341 (1970)

    Google Scholar 

  • Fishman, W. H., Green, S., Inglis, N. I.: Organ-specific behaviour exhibited by rat intestine and liver alkaline phosphatase. Biochim. biophys. Acta (Amst.) 62, 363–375 (1962)

    Google Scholar 

  • Graham, J. L., Grunbaum, B. W.: A rapid method for microelectrophoresis and quantitation of haemoglobins on cellulose acetate. Amer. J. clin. Path. 39, 567–578 (1963)

    Google Scholar 

  • Hviid, K.: An automated alkaline phosphatase assay with phenolphthalein monophosphate as substrate. Clin. Chem. 13, 281–289 (1967)

    Google Scholar 

  • Leroux, M. L., Perry, W. F.: Observations on the heat stability and electrophoretic patterns of alkaline phosphatases extracted from various tissues. Clin. Biochem. 8, 11–17 (1975)

    Google Scholar 

  • Lustig, V., Kellen, J. A.: Species, organ and subcellular specificity of alkaline phosphatases as determined by amino acid inhibition studies. Comp. Biochem. Physiol. 39B, 305–310 (1971)

    Google Scholar 

  • Moss, D. W.: Determination of intestinal alkaline phosphatase in serum by substrate-specificity measurements. Clin. chim. Acta 35, 413–419 (1971)

    Google Scholar 

  • Motzok, I., Branion, H. D.: Studies in alkaline phosphatases 2. Factors influencing pH optima and Michaelis constant. Biochem. J. 72, 177–183 (1959)

    Google Scholar 

  • Pickering, R. G.: Inexpensive apparatus for acrylamide gel electrophoresis in blocks. Lab. Pract. 25, 157–159 (1976)

    Google Scholar 

  • Poulik, M. D.: Starch gel electrophoresis in a discontinuous system of buffers. Nature (Lond.) 180, 1477–1479 (1957)

    Google Scholar 

  • Robinson, J. C., Pierce, J. E.: Differential action of neuraminidase on human serum alkaline phosphatases. Nature (Lond.) 204, 472–473 (1964)

    Google Scholar 

  • Ross, M. H., Ely, J. O., Archer, J. G.: Alkaline phosphatase activity and pH optima. J. biol. Chem. 192, 561–568 (1951)

    Google Scholar 

  • Saini, P. K., Posen, S.: The origin of serum alkaline phosphatase in the rat. Biochim. biophys. Acta (Amst.) 177, 42–49 (1969)

    Google Scholar 

  • Smith, I.: Chromatographicand electrophoretic techniques, Vol. II. Zone electrophoresis. 2nd Ed., pp. 217–237. London: Heinemann 1967

    Google Scholar 

  • Smith, I., Lighthouse, P. J., Perry, J. D.: Separation of human tissue alkaline phosphatases by electrophoresis on acrylamide disc gels. Clin. chim. Acta 19, 499–505 (1968)

    Google Scholar 

  • Smith, I., Perry, J. D., Lighthouse, P. J.: Disk electrophoresis of alkaline phosphatases from human serum and tissue extracts. Biochem. J. 105, 12p (1967)

  • Triantaphyllopoulos, E., Tuba, J.: Studies on the distribution and kinetics of the alkaline phosphatase of rat small intestine. Canad. J. Biochem. Physiol. 37, 699–708 (1959)

    Google Scholar 

  • Watson, W. C., Murray, E. S., Gardner, M. D.: Regulation of intestinal alkaline phoshatase levels in the rat. J. clin. Path. 20, 185–189 (1967)

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Shell Research Limited, Shell Toxicology Laboratory (Tunstall), Sittingbourne Research Centre, ME9 8AG, Sittingbourne, England

    C. E. Pickering & R. G. Pickering

Authors
  1. C. E. Pickering
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. R. G. Pickering
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Pickering, C.E., Pickering, R.G. Studies of rat alkaline phosphatase. Arch. Toxicol. 39, 249–266 (1978). https://doi.org/10.1007/BF00296386

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00296386

Key words

Search

Navigation