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Serum glycoproteins in the liver diseases

VI. The presence of desialylated glycoprotein binding activity in paniculate fraction of human liver homogenate

Summary

The human liver as well as rat liver particulate fraction was determined to have an ability to bind desialylated a1-acid glycoprotein. The binding activity of human liver was the same order of the rat one. A more increased amount of binding of desialylated glycoprotein was found in a new born liver than an adult one.

Serum obtained from a cirrhotic patient inhibited the binding. The sucrose density gradient centrifugation revealed that the activity located partly in fractions in which a membrane enzyme, alkaline phosphatase, was detected. The binding activity was a linear function of concentration of human liver particulate fraction added to incubation mixture.

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Arima, T., Kondo, T. & Nagashima, H. Serum glycoproteins in the liver diseases. Gastroenterol Jpn 13, 507–511 (1978). https://doi.org/10.1007/BF02774917

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  • DOI: https://doi.org/10.1007/BF02774917

Key Words

  • asialoglycoprotein receptor
  • human liver
  • rat liver
  • calcium chloride
  • sialic acid
  • liver cell membrane
  • liver particulate fraction
  • α1-acid glycoprotein
  • liver cirrhosis
  • sucrose density gradient centrifugation