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The Isolation and Properties of a Rabbit Liver Binding Protein Specific for Asialoglycoproteins
Open accessAbstract
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.
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Cited by
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Cuatrecasas, P., & Hollenberg, M. D. (1976) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60481-7 · Cited by 478
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Metadata
- Authors
- Hudgin, R. L., Pricer, W. E., Ashwell, G., Stockert, R. J., & Morell, A. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1974-09
- Volume
- 249
- Issue
- 17
- Pages
- 5536-5543
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1658581991
- Cited by
- 615
- References
- 0
- FWCI
- 11.50
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Hudgin, R. L., Pricer, W. E., Ashwell, G., Stockert, R. J., & Morell, A. G. (1974). The Isolation and Properties of a Rabbit Liver Binding Protein Specific for Asialoglycoproteins. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(20)79761-9
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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