The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A membrane protein from human erythrocytes involved in anion exchange
Open accessAbstract
Phosphate transport across the membrane of human erythrocytes, at pH 6.42, is a saturable process with an external Km of 80 mM and a Vmax of 2.8 mmol per liter of red cells per min. Transport is inhibited in a reversible manner by the sulfanilate anion and in an irreversible manner by the isothiocyanate derivative of the sulfanilate anion. This reagent reacts with only one membrane protein. When 300,000 molecules of reagent per cell are covalently attached to protein, transport is completely inhibited. This transport protein is a glycoprotein, it belongs to the general class designated as component a by Bretscher, and it therefore spans the bilayer. Transport does not involve movement of the protein around an axis parallel to the plane of the membrane.
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Citations
Cites
Colorimetric Method for Determination of Sugars and Related Substances
DuBois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., & Smith, F. (1956) · Analytical Chemistry · doi:10.1021/ac60111a017 · Cited by 52,269
Metadata
- Authors
- Ho, M. K., & Guidotti, G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1975-01
- Volume
- 250
- Issue
- 2
- Pages
- 675-683
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1585661349
- Cited by
- 257
- References
- 1
- FWCI
- 47.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.