The Isolation and Properties of a Rabbit Liver Binding Protein Specific for Asialoglycoproteins

The ability of hepatic plasma membranes to bind desialylated glycoproteins as a prelude to transport and catabolism has been reported earlier. The present study describes the purification, by affinity chromatography, of an hepatic protein which retains the characteristic binding properties associate...

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Bibliographic Details
Published in:The Journal of biological chemistry 1974-09, Vol.249 (17), p.5536-5543
Main Authors: Hudgin, R L, Pricer, Jr, W E, Ashwell, G, Stockert, R J, Morell, A G
Format: Article
Language:English
Subjects:
Acetone
Amino Acids - analysis
Animals
Binding Sites
Cattle
Cell Membrane - metabolism
Chromatography, Affinity
Chromatography, Gel
Clostridium perfringens - enzymology
Electrophoresis, Disc
Hexoses - analysis
Humans
Hydrogen-Ion Concentration
Iodine Radioisotopes
Kinetics
Liver - cytology
Liver - metabolism
Neuraminidase
Orosomucoid - metabolism
Pancreas - enzymology
Protein Binding
Proteins - isolation & purification
Proteins - metabolism
Rabbits
Receptors, Drug
Sialic Acids - analysis
Solubility
Trypsin
Ultracentrifugation
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Summary:The ability of hepatic plasma membranes to bind desialylated glycoproteins as a prelude to transport and catabolism has been reported earlier. The present study describes the purification, by affinity chromatography, of an hepatic protein which retains the characteristic binding properties associated with the membranes. The isolated material, which is watersoluble and free from lipids, has been identified as a glycoprotein in which 10 % of the dry weight consists of sialic acid, galactose, mannose, and glucosamine in a molar ratio of 1:1:2:2. The integrity of the terminal sialic acid residues and the presence of calcium were shown to be absolute requirements for binding. Physical chemical studies indicated a high degree of aggregation in the final, water-soluble preparation.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(20)79761-9