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Serum glycoproteins in the liver diseases. VII. Further studies on the properties of desialylated glycoprotein binding activity in particulate fraction of human liver homogenate

Gastroenterologia Japonica volume 14, pages 344–348 (1979)Cite this article

Summary

Binding of desialylated a1-acid glycoprotein by human liver particulate fraction exihibited a dependence on the presence of calcium chloride whereas Cu++, Mn++, Zn++ Fe++ and Co++ inhibited the binding. The other cations such as K+, Na+, Ba++, Mg++ or Pb++ were determined to be non-effective on the binding activity. The pH of the assay for binding was not critical in the range of 6.5 to 9.5. The binding process required the presence of terminal sialic acid on the particulate protein. Fifty nine per cent of binding activity in the original liver paticulate fraction were recovered in acetone powder. Extraction of the acetone powder with a buffer containing EDTA resulted in an increased total binding activity. After extraction with 1–10% Triton X-100, 60% of the activity were still detected in insoluble fraction.

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Authors and Affiliations

  1. The First Department of Internal Medicine, Okayama University Medical School, 700, Okayama, Japan

    Terukatsu Arima M.D.& D. SCI.

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  1. Terukatsu Arima M.D.& D. SCI.
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Arima, T. Serum glycoproteins in the liver diseases. VII. Further studies on the properties of desialylated glycoprotein binding activity in particulate fraction of human liver homogenate. Gastroenterol Jpn 14, 344–348 (1979). https://doi.org/10.1007/BF02774231

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  • DOI: https://doi.org/10.1007/BF02774231

Key Words

  • desialylated glycoproteins
  • α1-acid glycoprotein
  • human liver
  • rat liver
  • calcium chloride
  • neuraminidase
  • sialic acid
  • EDTA
  • Triton X-100
  • acetone