PMID: 39866Aug 1, 1979

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
T Arima

Abstract

Binding of desialylated alpha 1-acid glycoprotein by human liver particulate fraction exhibited 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.

References

Aug 21, 1972·Biochemical and Biophysical Research Communications·A G Morell, I H Scheinberg
Mar 1, 1969·The Journal of Experimental Medicine·J J Woodruff, B M Gesner
Jul 15, 1962·Proceedings of the National Academy of Sciences of the United States of America·G GASIC, T GASIC
Sep 1, 1965·The Journal of Cell Biology·L Weiss

Related Concepts

Metazoa
Cations, Divalent
Edetic Acid, Calcium, Sodium Salt
Neoglycoproteins
Hydrogen-Ion Concentration
Liver
Neuraminidase
Vigilon
Plasma Protein Binding Capacity
Polysialoglycoproteins

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