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Gastroenterologia Japonica

, Volume 10, Issue 4, pp 283–289 | Cite as

Comparison of detectability of elevated amylase of serum and urine in pancreatic diseases by two amylase assay methods using starch substrates of different digestive rates to pancreatic amylase

  • Tetsuo Hayakawa
  • Yasushi Toda
  • Saburo Nakazawa
  • Aiji Noda
  • Frank F. Hall
  • Nicholas C. Hightower
Original Article
  • 38 Downloads

Summary

Detectability of abnormally high serum and urine amylases was investigated on patients with pancreatic diseases using amylase assays with substrates of different digestive rates to pancreatic amylase. Ratios of amylase activities determined by a chromogenic assay using a Remazolbrilliant Blue R starch (RBB assay) to those by Caraway’s assay using a Lintner soluble starch (R/C ratio) were calculated on duodenal and salivary amylases obtained from 16 subjects undergoing a pancreozymin-secretin test. The R/C ratio of the duodenal amylase (M ±SD = 0.56 ±0.12) was significantly higher (p<0.01 by F test) than that of the salivary amylase (M ±SD = 0.36 ±0.10). Detectability of above-normal values of serum and urine amylases were compared with two assays in 77 pancreatic patients. The value for serum and urine amylases determined by the RBB and Caraway’s assays exceeded the upper limit of normal in 37 and 58% by the RBB assay and 24 and 26% by Caraway’s assay, respectively. Degrees of abnormality (ratio of the observed to the upper normal value) in serum and urine amylases were also significantly higher (p<0.05 for serum and p<0.01 upper for urine) by the RBB assay than by Caraway’s assay. The RBB assay was more sensitive than Caraway’s assay in detecting elevation of pancreatic amylase in serum and urine.

Key words

pancreatic amylase salivary amylase serum amylase urine amylase chromogenic method Caraway’s method digestive rate of starch substrate 

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References

  1. 1).
    Nørby, S.: Electrophoretic non-identity of human salivary and pancreatic amylases. Exp. Cell Res. 36: 663–666, 1964.PubMedCrossRefGoogle Scholar
  2. 2).
    Aw, S.E. and Hobbs, J.R.: Human isoamylases. Biochem. J. 99: 16p, 1966.Google Scholar
  3. 3).
    Hayakawa, T., Hall, F.F. and Hightower, N.C.: Mechanism of amylase inhibition by antibody. Gastroenterology 58: 1059, 1970.Google Scholar
  4. 4).
    Hall, F.F., Ratliff, C.R., Hayakawa, T., et al.: Substrate differentiation of human pancreatic and salivary alpha-amylases. Am. J. Dig. Dis. 15: 1031–1038, 1970.PubMedCrossRefGoogle Scholar
  5. 5).
    Hayakawa, T., Toda, Y., Noda, A., et al.: Substrate differentiation of human pancreatic and salivary amylases and its clinical application. Jap. J. Gastroenterology 70: 485–490, 1973.Google Scholar
  6. 6).
    Meites, S. and Rogols, S.: Serum amylases, isoenzymes, and pancreatitis. 1. Effect of substrate variation. Clin. Chem. 14: 1176–1184, 1968.PubMedGoogle Scholar
  7. 7).
    Caraway, W.T.: A stable starch substrate for the determination of amylase in serum and other body fluids. Am. J. Clin. Path. 32: 97–99, 1959.PubMedGoogle Scholar
  8. 8).
    Rinderknecht, H., Wilding, P. and Haverback, B.J.: A new method for the determination of α-amylase. Experientia 23: 805–806, 1967.PubMedCrossRefGoogle Scholar
  9. 9).
    Hall, F.F., Culp, T.W., Hayakawa, T., et al.: An improved amylase assay using a new starch derivative. Am. J. Clin. Path. 53: 627–634, 1970.PubMedGoogle Scholar

Copyright information

© The Japanese Society of Gastroenterology 1975

Authors and Affiliations

  • Tetsuo Hayakawa
    • 1
  • Yasushi Toda
    • 1
  • Saburo Nakazawa
    • 1
  • Aiji Noda
    • 1
  • Frank F. Hall
    • 2
  • Nicholas C. Hightower
    • 2
  1. 1.2nd Dept. of Internal MedicineNagoya University School of MedicineNagoyaJapan
  2. 2.Scott and White ClinicTempleUSA

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