Purification and characterization of a lectin from Wistaria floribunda seeds.
Open accessAbstract
A lectin from Wistaria floribunda seeds which specifically binds to N-acetyl-D-galactosamine was purified to homogeneity as judged by polyacrylamide gel electrophoresis. Its molecular weight was estimated to be 68,000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. It dissociated into subunits on reduction with 2-mercaptoethanol with concomitant loss of hemagglutinating activity. On oxidation in air, the subunits reassociated into the lectin molecules with hemagglutinating activity. Carboxymethylation of the subunits with iodoacetic acid prevented their reassociation on oxidation in air. The molecular weight of the subunits was 32,000, which is about one-half that of the native lectin, suggesting that the lectin consists of two subunits. The results total, NH2-terminal, and COOH-terminal amino acid analyses, and mapping of the tryptic digest of the lectin indicated that these two subunits were indistinguishable and were probably identical, and that they were linked together covalently through a single disulfide bond. Equilibrium dialysis experiments show that the lectin and its subunit molecules are divalent and monovalent, respectively, with respect to sugar binding. The lectin is a glycoprotein, containing 3.2% carbohydrate. The carbohydrate moiety is composed of mannose, galactose, and glucosamine is a molar ratio of 1:2:1 and these sugars seem to be linked as a single oligosaccharide chain to each subunit of the protein.
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The specific binding site for WFA is known.
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Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Colorimetric Method for Determination of Sugars and Related Substances
DuBois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., & Smith, F. (1956) · Analytical Chemistry · doi:10.1021/ac60111a017 · Cited by 52,269 · see citing works
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,383 · see citing works
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 19,724 · see citing works
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 16,688 · see citing works
Automatic recording apparatus for use in the chromatography of amino acids.
Moore, S., Spackman, D., & Stein, W. (1958) · Federation proceedings · doi:10.1021/ac60139a006 · Cited by 8,126 · see citing works
Estimation of the molecular weights of proteins by Sephadex gel-filtration
Andrews, P. (1964) · Biochemical Journal · doi:10.1042/bj0910222 · Cited by 3,903 · see citing works
On the Determination of Cystine as Cysteic Acid
Moore, S. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83985-6 · Cited by 3,013 · see citing works
Udenfriend, S., Stein, S., Böhlen, P., Dairman, W. M., Leimgruber, W., & Weigele, M. (1972) · Science · doi:10.1126/science.178.4063.871 · Cited by 2,639 · see citing works
The Preparation and Enzymatic Hydrolysis of Reduced and S-Carboxymethylated Proteins
Crestfield, A. M., Moore, S., & Stein, W. H. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81308-4 · Cited by 2,587 · see citing works
Hedrick, J. L., & Smith, A. J. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90569-9 · Cited by 1,901 · see citing works
Lectins: Cell-Agglutinating and Sugar-Specific Proteins
Sharon, N., & Lis, H. (1972) · Science · doi:10.1126/science.177.4053.949 · Cited by 1,711 · see citing works
The spectrophotometric determination of tyrosine and tryptophan in proteins.
Goodwin, T., & Morton, R. A. (1946) · Biochemical Journal · doi:10.1042/bj0400628 · Cited by 1,157 · see citing works
Goldstein, I. J., Hollerman, C. E., & Smith, E. E. (1965) · Biochemistry · doi:10.1021/bi00881a013 · Cited by 847 · see citing works
[12] Dansyl chloride procedure
Gray, W. R. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(67)11014-8 · Cited by 652 · see citing works
Amino-terminal Sequence Analysis of Proteins Purified on a Nanomole Scale by Gel Electrophoresis
Weiner, A. M., Platt, T., & Weber, K. K. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45237-x · Cited by 648 · see citing works
The Covalent and Three-Dimensional Structure of Concanavalin A
Edelman, G. M., Cunningham, B. A., Reeke, G. N., et al. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.9.2580 · Cited by 540 · see citing works
A Sphingolipid Having a Novel Type of Ceramide and Lacto-N-Fucopentaose III
Yang, H.-J., & Hakomori, S. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)76958-0 · Cited by 484 · see citing works
Rapid Paper Chromatography or Carbohydrates and Related Compounds
Gordon, H. T., Thornburg, W., & Werum, L. N. (1956) · Analytical Chemistry · doi:10.1021/ac60113a020 · Cited by 377 · see citing works
Thin-layer chromatography of PTH amino acids
Jeppsson, J., & Sjöquist, J. (1967) · Analytical Biochemistry · doi:10.1016/0003-2697(67)90009-7 · Cited by 296 · see citing works
[14] Enzymic hydrolysis with carboxypeptidases
Ambler, R. P. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(67)11016-1 · Cited by 225 · see citing works
Unusual Fragments in the Subunit Structure of Concanavalin A
Wang, J. L., Cunningham, B. A., & Edelman, G. M. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.6.1130 · Cited by 221 · see citing works
The molecular weight and stability of concanavalin A
McKenzie, G. H., Sawyer, W. H., & Nichol, L. W. (1972) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(72)90081-5 · Cited by 182 · see citing works
Sjöquist, J. (1960) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(60)90364-4 · Cited by 162 · see citing works
A reinvestigation of the hydrazinolytic procedure for the determination of C-terminal amino acids
Braun, V., & Schroeder, W. A. (1967) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(67)90303-7 · Cited by 145 · see citing works
Soybean Hemagglutinin, a Plant Glycoprotein
Lis, H., Sharon, N., & Katchalski, E. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96892-4 · Cited by 140 · see citing works
Separation of proteins by ammonium sulfate gradient solubilization
King, T. P. (1972) · Biochemistry · doi:10.1021/bi00753a010 · Cited by 140 · see citing works
Matsuo, H., Fujimoto, Y., & Tatsuno, T. (1966) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(66)90604-8 · Cited by 122 · see citing works
Toyoshima, S., & OSAWA, T. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41743-2 · Cited by 104 · see citing works
Matsumoto, I., & Osawa, T. (1970) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(70)90092-5 · Cited by 101 · see citing works
Phytomitogen from Wistaria floribunda seeds and its interaction with human peripheral lymphocytes
Toyoshima, S., Akiyama, Y., Nakano, K., et al. (1971) · Biochemistry · doi:10.1021/bi00800a016 · Cited by 77 · see citing works
Phosphoglucomutase. V. Multiple forms of phosphoglucomutase.
Joshi, J. G., Hooper, J. A., Kuwaki, T., et al. (1967) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.57.5.1482 · Cited by 49 · see citing works
The Anti-N Lectin of Bauhinia Purpurea
Boyd, W. C., Everhart, D. L., & McMaster, M. H. (1958) · The Journal of Immunology · doi:10.4049/jimmunol.81.5.414 · Cited by 45 · see citing works
On the surface structure of murine ascites tumors. I. Interactions with various phytoagglutinins
Tomita, M., Osawa, T., Sakurai, Y., et al. (1970) · International Journal of Cancer · doi:10.1002/ijc.2910060216 · Cited by 45 · see citing works
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- Authors
- Kurokawa, T., Tsuda, M., & Sugino, Y.
- Affiliations
- Takeda (Japan) (JP)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1976-09
- Volume
- 251
- Issue
- 18
- Pages
- 5686-5693
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1600919994
- Cited by
- 82
- References
- 34
- Citations by year
- 2026: 4 · 2025: 1 · 2024: 2 · 2022: 1 · 2021: 3 · 2020: 6 · 2019: 2 · 2018: 2 · 2017: 7 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 1 · 2012: 3
- FWCI
- 0.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
- Life Sciences › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
- Keywords
- lectins, seed lectin, lectin purification, disulfide bonds, subunit structure, glycoproteins, oligosaccharides, carbohydrate composition, hemagglutination
- MeSH terms
- Amino Acid Sequence, Amino Acids, Animals, Glucosamine, Hemagglutination Tests, Hexoses, Humans, Molecular Weight, Oxidation-Reduction, Peptide Fragments, Seeds, Species Specificity, Trypsin, Lectins, Plant Lectins, Macromolecular Substances
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