The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Wheat Germ Agglutinin
Open accessAbstract
Abstract Crystalline wheat germ agglutinin was prepared from unprocessed wheat germ by a new purification procedure. Its purity and some of its molecular characteristics were examined by a number of criteria. Sedimentation analysis gave a molecular weight of 17,000 ± 1,000 and a sedimentation coefficient of 2.1 S when determined in 0.05 n HCl. At neutral pH, the agglutinin dimerizes with a molecular weight of around 35,000 and a sedimentation coefficient of 3.6 S. Amino acid analyses indicate that the protein contains a high amount of glycine and half-cystine; none of the latter is present as cysteine. Three times crystallized agglutinin is devoid of neutral sugars. Equilibrium dialysis experiments using N-acetyl-[1-14C]glucosamine indicate that the agglutinin has 2-binding sites for N-acetylglucosamine per mole of the polypeptide chain with a dissociation constant of 7.6 x 10-4 m. This binding is highly specific. The β-1,4 di- and trisaccharides of N-acetylglucosamine showed higher affinities with apparent dissociation constants of 4.9 and 1.2 x 10-5 m, respectively.
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Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 20,298
THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
Scatchard, G. (1949) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1949.tb27297.x · Cited by 19,778
Bray, G. A. (1960) · Analytical Biochemistry · doi:10.1016/0003-2697(60)90025-7 · Cited by 7,476
THE OXIDATION OF RIBONUCLEASE WITH PERFORMIC ACID
Hirs, C. H. W. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65721-7 · Cited by 1,857
Sharon, N., & Lis, H. (1972) · Science · doi:10.1126/science.177.4053.949 · Cited by 1,706
Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic Mercurials
Boyer, P. D. (1954) · Journal of the American Chemical Society · doi:10.1021/ja01646a025 · Cited by 1,667
A SUBMICRODETERMINATION OF GLUCOSE
Park, J. T., & Johnson, M. J. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)56635-7 · Cited by 1,570
The spectrophotometric determination of tyrosine and tryptophan in proteins
Goodwin, T. W., & Morton, R. A. (1946) · Biochemical Journal · doi:10.1042/bj0400628 · Cited by 1,514
Determination of Tyrosine and Tryptophan in Proteins
Bencze, W. L., & Schmid, K. (1957) · Analytical Chemistry · doi:10.1021/ac60128a025 · Cited by 757
A DIFFERENCE IN THE ARCHITECTURE OF THE SURFACE MEMBRANE OF NORMAL AND VIRALLY TRANSFORMED CELLS
Burger, M. M. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.62.3.994 · Cited by 549
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Ensign, L. M., Cone, R., & Hanes, J. (2012) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2011.12.009 · Cited by 1,623
The Lectins: Carbohydrate-Binding Proteins of Plants and Animals
Goldstein, I. J., & Hayes, C. E. (1978) · Advances in Carbohydrate Chemistry and Biochemistry · doi:10.1016/s0065-2318(08)60220-6 · Cited by 1,621
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Metadata
- Authors
- Nagata, Y., & Burger, M. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1974-05
- Volume
- 249
- Issue
- 10
- Pages
- 3116-3122
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1560194095
- Cited by
- 606
- References
- 23
- FWCI
- 11.50
- 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.
