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Cited by 451

The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.

The size and detergent binding of membrane proteins.

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Clarke, S·1975·Journal of Biological Chemistry

Abstract

Sucrose density gradient centrifugation has been used to measure the binding of Triton X-100 above its critical micellar concentration to a variety of purified membrane and non-membrane proteins. In addition, binding studies were done on the three proteins below the critical micellar concentration of detergent to distinguish between the interaction of proteins with detergent monomers and detergent micelles. A procedure is described for the calculation of the molecular weight of these Triton X-100 protein complexes and measurements were made for opsin, plasma low density lipoprotein, the (Na-+ plus K-+)-dependent adenosine triphosphatase, the human red blood cell major sialoglycoprotein (PAS-1) and the human red blood cell minor glycoprotein (bandIII). These proteins behave as monomers or dimers in detergent and bind between 0.28 and 1.12 g of detergent per g of protein. A general method is also present for calculating the molecular size and shape of impure membrane proteins in detergent. Finally, Triton X-100 was shown to replace bound Na dodecyl-SO4 on the minor glycoprotein of the red blood cell.

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Metadata

Authors
Clarke, S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1975-07
Volume
250
Issue
14
Pages
5459-5469
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1608638180
Cited by
451
References
29
FWCI
14.55
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The size and detergent binding of membrane proteins. https://app.cochat.ai/papers/10.1016/s0021-9258(19)41204-0
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Clarke, S. (1975). The size and detergent binding of membrane proteins. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)41204-0

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