The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Properties of the Two Polypeptides of Sodium- and Potassium-dependent Adenosine Triphosphatase
Open accessAbstract
Abstract The (Na+ + K+)-dependent adenosine triphosphatase from canine renal medulla is composed of lipids and of two polypeptide chains. The larger one has a molecular weight of 135,000, NH2-terminal glycine, and has a high content of non-polar amino acids. The smaller polypeptide chain has NH2-terminal alanine and it is a sialoglycoprotein. The two polypeptides are present in a mass ratio of 1.7:1 for the ratio of large to small chain. This mass ratio probably corresponds to a molar ratio of one large chain to two small chains. The two chains are close to one another in the purified enzyme because they can be covalently crosslinked by dimethyl suberimidate. Finally, the large polypeptide chain, which has all of the properties of a membrane-bound enzyme, is soluble in simple aqueous solvents in the absence of detergents and lipids, although it no longer has enzymatic activity.
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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
- Kyte, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1972-12
- Volume
- 247
- Issue
- 23
- Pages
- 7642-7649
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1577284422
- Cited by
- 265
- References
- 1
- FWCI
- 11.13
- 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.
