The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
The Binding of Detergents to Lipophilic and Hydrophilic Proteins
Open accessAbstract
Abstract The lipophilic protein moieties of human low density lipoprotein, Semliki Forest virus envelope, and human erythrocyte stroma were obtained lipid-free with the use of sodium deoxycholate treatment and gel filtration in deoxycholate-containing media. Detergent binding was determined by subjecting the proteins to gel filtration in the presence of micellar concentrations of radioactive deoxycholate or the nonionic detergent Triton X-100. The amount of detergents bound to the proteins could be measured from the amount of radioactive detergent that co-eluted with the protein. The lipophilic proteins bound large amounts of deoxycholate and Triton X-100 (up to about 70% of their weight). The hydrophilic proteins tested bound little or no deoxycholate or Triton X-100.
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Metadata
- Authors
- Helenius, A., & Simons, K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1972-06
- Volume
- 247
- Issue
- 11
- Pages
- 3656-3661
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1599125820
- Cited by
- 358
- References
- 17
- FWCI
- 12.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
