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Cited by 764

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

A one-step purification of membrane proteins using a high efficiency immunomatrix.

Open access
Schneider, C, Newman, R A, Sutherland, D R, Asser, U, Greaves, M F·1982·Journal of Biological Chemistry

Abstract

A method is described by which an immunoaffinity matrix was constructed by binding antibody directly or indirectly to protein A-Sepharose 4B followed by cross-linking of the complex with dimethyl pimelimidate. This allows optimal spatial orientation of antibodies and, thus, maximum antigen binding efficiency. The affinity matrices were stable to high and low pH buffers without any significant antibody loss. The optimal conditions of antibody saturation, cross-linker concentration, and elution system were established and affinity columns made with the monoclonal antibodies J5, W6/32, and OKT9 for one-step isolation of the common acute lymphoblastic leukemia-associated antigen, HLA-AB antigens, and transferrin receptor, respectively, from cell lysates. The same methodology was also applied to immobilize transferrin with polyvalent anti-transferrin antibodies. This was then used to isolate the transferrin receptor from cell lysates.

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Metadata

Authors
Schneider, C., Newman, R. A., Sutherland, D. R., Asser, U., & Greaves, M. F.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1982-09
Volume
257
Issue
18
Pages
10766-10769
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1528710182
Cited by
764
References
2
FWCI
6.71
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: A one-step purification of membrane proteins using a high efficiency immunomatrix. https://app.cochat.ai/papers/10.1016/s0021-9258(18)33889-4
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Schneider, C., Newman, R. A., Sutherland, D. R., Asser, U., & Greaves, M. F. (1982). A one-step purification of membrane proteins using a high efficiency immunomatrix. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)33889-4

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.