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Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric Proteins
Open accessAbstract
Amidination of aldolase, glyceraldehyde-3-phosphate dehydrogenase, tryptophan synthetase B protein, L-arabinose isomerase, and the catalytic subunit of E. coli aspartate transcarbamylase with the bifunctional reagent dimethyl suberimidate produces cross-linked proteins, with reaction predominating within oligomers. Disc electrophoresis of a modified protein on polyacrylamide gel in the presence of sodium dodecyl sulfate resolves a set of species with molecular weights equal to integral multiples of the protomer molecular weight. For oligomers composed of identical protomers, the number of principal species observed is identical to the number of protomers in the oligomer. Application of the method to two proteins composed of dissimilar protomers, native aspartate transcarbamylase and tryptophan synthetase α 2 β 2 complex of E. coli , revealed differences in the reactivities of the different kinds of protomer within each oligomer.
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Cited by
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Klee, C. B., Crouch, T. H., & Krinks, M. H. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.12.6270 · Cited by 579
The size and detergent binding of membrane proteins.
Clarke, S. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41204-0 · Cited by 451
Properties of an interphotoreceptor retinoid-binding protein from bovine retina
Saari, J. C., Teller, D. C., Crabb, J. W., & Bredberg, L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89715-0 · Cited by 120
Glutamate dehydrogenase from Escherichia coli: purification and properties
Sakamoto, N., Kotre, A. M., & Savageau, M. A. (1975) · Journal of Bacteriology · doi:10.1128/jb.124.2.775-783.1975 · Cited by 119
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Metadata
- Authors
- Davies, G. E., & Stark, G. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1970-07
- Volume
- 66
- Issue
- 3
- Pages
- 651-656
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2018244729
- Cited by
- 823
- References
- 0
- FWCI
- 20.79
- Type
- journal article
- Language
- en
- Open access
- green
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