The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The structure and stability of human plasma cold-insoluble globulin.
Open accessAbstract
The molecular properties of cold-insoluble globulin have been investigated by velocity centrifugation, circular dichroism, and fluorescence at neutral and alkaline pH. The stability of the protein to thermal and guanidine hydrochloride has been evaluated under both conditions. The close parallelism between the properties of cold-insoluble globulin and those of the cell surface protein (fibronectin) serve to establish the essential identity of the structures of the two proteins derived from different sources. It is suggested that the cold-insoluble globulin is composed of several domains connected by flexible polypeptide segments. The large increase in the frictional ratio observed between pH 7.0 and 11.0 can be explained by an expansion of the flexible segments without significant change in the domains. These domains are stable to about 55 degrees C at pH 7.0 but only to about 40 degrees C at pH 11.0.
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Citations
Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Cited by
Engel, J., Odermatt, E., Engel, A., Madri, J. A., Furthmayr, H., Rohde, H., & Timpl, R. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90326-0 · Cited by 667
Force-Induced Unfolding of Fibronectin in the Extracellular Matrix of Living Cells
Smith, M. L., Gourdon, D., Little, W. C., Kubow, K. E., Eguiluz, R. A., Luna-Morris, S., & Vogel, V. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050268 · Cited by 440
Degradation of fibronectin by human leukocyte elastase. Release of biologically active fragments.
McDonald, J. A., & Kelley, D. G. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43580-6 · Cited by 381
Adsorption characteristics of plasma fibronectin in relationship to biological activity
Grinnell, F., & Feld, M. K. (1981) · Journal of Biomedical Materials Research · doi:10.1002/jbm.820150308 · Cited by 329
Rapid methods for isolation of human plasma fibronectin
Miekka, S. I., Ingham, K. C., & Menache, D. (1982) · Thrombosis Research · doi:10.1016/0049-3848(82)90272-9 · Cited by 310
Metadata
- Authors
- Alexander, S. S., Colonna, G., & Edelhoch, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1979-03
- Volume
- 254
- Issue
- 5
- Pages
- 1501-1505
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1559834502
- Cited by
- 177
- References
- 1
- FWCI
- 8.34
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Alexander, S. S., Colonna, G., & Edelhoch, H. (1979). The structure and stability of human plasma cold-insoluble globulin. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)37797-9
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
