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Isolation and characterization of a phytohemagglutinin from the lentil

Cite this: Biochemistry 1969, 8, 6, 2436–2441
Publication Date (Print):June 1, 1969
https://doi.org/10.1021/bi00834a028
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    3. Mariam V. Mikaelyan, Gayane G. Poghosyan, Olga D. Hendrickson, Boris B. Dzantiev, Vardan K. Gasparyan. Wheat germ agglutinin and Lens culinaris agglutinin sensitized anisotropic silver nanoparticles in detection of bacteria: A simple photometric assay. Analytica Chimica Acta 2017, 981 , 80-85. https://doi.org/10.1016/j.aca.2017.05.022
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    5. Atul Gajanan Thawari, Khatija Tabbasum, Vijaya Kumar Hinge, Chebrolu Pulla Rao. Pb 2+ binding to lentil lectin and its influence on the protein aggregation. RSC Advances 2015, 5 (88) , 72352-72360. https://doi.org/10.1039/C5RA06427A
    6. AU Hivrale, AG Ingale. Plant as a plenteous reserve of lectin. Plant Signaling & Behavior 2013, 8 (12) , e26595. https://doi.org/10.4161/psb.26595
    7. Tomohiro Suzuki, Kozue Sugiyama, Hirofumi Hirai, Hiroyuki Ito, Tatsuya Morita, Hideo Dohra, Takeomi Murata, Taichi Usui, Hiroaki Tateno, Jun Hirabayashi, Yuka Kobayashi, Hirokazu Kawagishi. Mannose-specific lectin from the mushroom Hygrophorus russula. Glycobiology 2012, 22 (5) , 616-629. https://doi.org/10.1093/glycob/cwr187
    8. Thomas Iskratsch, Andreas Braun, Katharina Paschinger, Iain B.H. Wilson. Specificity analysis of lectins and antibodies using remodeled glycoproteins. Analytical Biochemistry 2009, 386 (2) , 133-146. https://doi.org/10.1016/j.ab.2008.12.005
    9. Farah Naseem, Rizwan Hasan Khan. Fluoroalcohol-induced stabilization of the α-helical intermediates of lentil lectin: implication for non-hierarchical lectin folding. Archives of Biochemistry and Biophysics 2004, 431 (2) , 215-223. https://doi.org/10.1016/j.abb.2004.07.029
    10. María J. Marcos, Enrique Villar, Francisco Gavilanes, Galina G. Zhadan, Valery L. Shnyrov. Compact residual structure in lentil lectin at pH 2. European Journal of Biochemistry 2000, 267 (7) , 2127-2132. https://doi.org/10.1046/j.1432-1327.2000.01233.x
    11. Marı́a J. Marcos, Rosana Chehı́n, Jose L. Arrondo, Galina G. Zhadan, Enrique Villar, Valery L. Shnyrov. pH‐dependent thermal transitions of lentil lectin. FEBS Letters 1999, 443 (2) , 192-196. https://doi.org/10.1016/S0014-5793(98)01708-6
    12. Mustapha Hajjou, Yves Le Gal. Purification and characterization of an aminopeptidase from tuna (Thunnus albacares) pyloric caeca. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1994, 1204 (1) , 1-13. https://doi.org/10.1016/0167-4838(94)90025-6
    13. Ramesh HEGDE, Sunil K. PODDER. Studies on the variants of the protein toxins ricin and abrin. European Journal of Biochemistry 1992, 204 (1) , 155-164. https://doi.org/10.1111/j.1432-1033.1992.tb16618.x
    14. Ramesh Hegde, T.K. Maiti, S.K. Podder. Purification and characterization of three toxins and two agglutinins from Abrus precatorius seed by using lactamyl-Sepharose affinity chromatography. Analytical Biochemistry 1991, 194 (1) , 101-109. https://doi.org/10.1016/0003-2697(91)90156-N
    15. Milan Bier, Terry Long, Hwa-Won Ryu. Separation of Lens culinaris Hemagglutinin by Forced Flow Electrophoresis. Separation Science and Technology 1990, 25 (9-10) , 997-1005. https://doi.org/10.1080/01496399008050380
    16. R.S. Bhatty. Composition and Quality of Lentil (Lens culinaris Medik): A Review. Canadian Institute of Food Science and Technology Journal 1988, 21 (2) , 144-160. https://doi.org/10.1016/S0315-5463(88)70770-1
    17. Pierre Wenger, Ariane Heydt, Ned B. Egen, Terry D. Long, Milan Bier. Purification of lentil lectins using preparative electrophoresis. Journal of Chromatography A 1988, 455 , 225-239. https://doi.org/10.1016/S0021-9673(01)82121-X
    18. SHASHIKALA R. INAMDAR, B. MURUGISWAMY, M MADAIAH. Purification and characterization of a lectin from Euphorbia nivulia Buch. Ham. latex. International Journal of Peptide and Protein Research 1988, 31 (1) , 35-46. https://doi.org/10.1111/j.1399-3011.1988.tb00004.x
    19. R. Chandrika, M. S. Shaila. Isolation and properties of a lectin from the seeds ofMimosa invisa L.. Journal of Biosciences 1987, 12 (4) , 383-391. https://doi.org/10.1007/BF02898587
    20. I. T. I. Nojimoto, S. Hoshino-Shimizu, T. K. Nagasse-Sugahara, M. E. Camargo. Lectins for the detection of IgM antibodies to T. gondii in the diagnosis of acute toxoplasmosis by immunofluorescence test. Revista do Instituto de Medicina Tropical de São Paulo 1987, 29 (6) , 354-360. https://doi.org/10.1590/S0036-46651987000600004
    21. Prakash M. Dey, Surbhi Naik, John B. Pridham. Further characterization of α-galactosidase I-glycoprotein lectin from Vicia faba seeds. Phytochemistry 1986, 25 (5) , 1035-1041. https://doi.org/10.1016/S0031-9422(00)81549-6
    22. IRWIN J. GOLDSTEIN, RONALD D. PORETZ. Isolation, Physicochemical Characterization, and Carbohydrate-Binding Specificity of Lectins. 1986, 33-247. https://doi.org/10.1016/B978-0-12-449945-4.50007-5
    23. . References. 1985, 433-455. https://doi.org/10.1016/S0075-7535(08)70233-X
    24. L. Gualandris, P. Rougé, A. M. Duprat. Membrane changes in neural target cells studied with fluorescent lectin probes. Development 1983, 77 (1) , 183-200. https://doi.org/10.1242/dev.77.1.183
    25. Bjern Solheim. Purification and characterization of lectins from Vicia hirsuta. Physiologia Plantarum 1983, 58 (4) , 515-522. https://doi.org/10.1111/j.1399-3054.1983.tb05736.x
    26. M. A. Jacquet, A. Sharif. A microquantitative method for investigating the interaction between labeled lectins and the surface membranes of human lymphocytes using a semi-automatic harvesting machine. Experientia 1983, 39 (1) , 123-126. https://doi.org/10.1007/BF01960666
    27. P M Dey, E M Del Campillo, R P Lezica. Characterization of a glycoprotein alpha-galactosidase from lentil seeds (Lens culinaris).. Journal of Biological Chemistry 1983, 258 (2) , 923-929. https://doi.org/10.1016/S0021-9258(18)33139-9
    28. Lokesh Bhattacharyya, Pradip Kumar Das, A. Sen. Purification and properties of d-galactose-binding lectins from some erythrina species: Comparison of properties of lectins from E. indica, E. arborescens, E. suberosa, and E. lithosperma. Archives of Biochemistry and Biophysics 1981, 211 (1) , 459-470. https://doi.org/10.1016/0003-9861(81)90478-1
    29. J.‐O. Karlsson. Proteins of Rapid Axonal Transport: Polypeptides Interacting with the Lectin from Lens Culinavis. Journal of Neurochemistry 1980, 34 (5) , 1184-1190. https://doi.org/10.1111/j.1471-4159.1980.tb09958.x
    30. Jerry W. Pickering, Michael Wolcott. Some Structural Properties of Thymus Leukemia Antigen (TL) Solubilized with Detergent 1. Tissue Antigens 1979, 14 (3) , 261-269. https://doi.org/10.1111/j.1399-0039.1979.tb00848.x
    31. John Howard, Juanita Kindinger, Leland M. Shannon. Conservation of antigenic determinants among different seed lectins. Archives of Biochemistry and Biophysics 1979, 192 (2) , 457-465. https://doi.org/10.1016/0003-9861(79)90115-2
    32. Eugene J. Smith, Lyman B. Crittenden, Aurora K. Whitson. Radioimmunoassay for the envelope glycoprotein of subgroup E avian leukosis-sarcoma viruses. Virology 1978, 84 (2) , 331-340. https://doi.org/10.1016/0042-6822(78)90252-0
    33. G. L. Nicolson. Ultrastructural Localization of Lectin Receptors. 1978, 1-38. https://doi.org/10.1007/978-3-642-66809-8_1
    34. J�rgen Roth, Maximillian Binder, Uwe Jens Gerhard. Conjugation of lectins with fluorochromes: An approach to histochemical double labeling of carbohydrate components. Histochemistry 1978, 56 (3-4) , 265-273. https://doi.org/10.1007/BF00495988
    35. Irwin J. Goldstein, Colleen E. Hayes. The Lectins: Carbohydrate-Binding Proteins of Plants and Animals. 1978, 127-340. https://doi.org/10.1016/S0065-2318(08)60220-6
    36. Jay C. Brown, Richard C. Hunt. Lectins. 1978, 277-349. https://doi.org/10.1016/S0074-7696(08)60758-5
    37. . Chapter 11 Examples of the use of affinity chromatography. 1978, 245-363. https://doi.org/10.1016/S0301-4770(08)60584-9
    38. Elvin A. Kabat. Dimensions and specificities of recognition sites on lectins and antibodies. Journal of Supramolecular Structure 1978, 8 (1) , 79-88. https://doi.org/10.1002/jss.400080107
    39. Howard J. Allen, Edward A.Z. Johnson. Isolation and partial characterization of a lectin from Vicia faba. Biochimica et Biophysica Acta (BBA) - General Subjects 1976, 444 (2) , 374-385. https://doi.org/10.1016/0304-4165(76)90381-0
    40. R. Yanagimachi, G.L. Nicolson. Lectin-binding properties of hamster egg zona pellucida and plasma membrane during maturation and preimplantation development. Experimental Cell Research 1976, 100 (2) , 249-257. https://doi.org/10.1016/0014-4827(76)90145-2
    41. Klaus Thoss, J�rgen Roth. Histochemical lectin affinity technique by means of FITC-labeled serum protein fractions. Histochemistry 1976, 49 (1) , 67-72. https://doi.org/10.1007/BF00490127
    42. A. Sharif, R. Bourrillon. Human peripheral lymphocyte transformation induced by the Robinia lectin. Cellular Immunology 1975, 19 (2) , 372-380. https://doi.org/10.1016/0008-8749(75)90219-1
    43. D. Fialová, M. Tichá, J. Kocourek. Studies on phytohemagglutinins XXVI. A new type of a lentil hemagglutinin isolated from Lens esculenta Moench., subsp. Microsperma (Baumg.) Barulina. Biochimica et Biophysica Acta (BBA) - Protein Structure 1975, 393 (1) , 170-181. https://doi.org/10.1016/0005-2795(75)90228-7
    44. J. Roth. Electron microscopic demonstration of saccharide moieties in the hypophase of the alveolar surfactant system. Respiration Physiology 1975, 23 (3) , 325-335. https://doi.org/10.1016/0034-5687(75)90083-3
    45. Rokuro Kaifu, Toshiaki Osawa, Roger W. Jeanloz. Synthesis of 2-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-D-mannose, and its interaction with D-mannose-specific lectins. Carbohydrate Research 1975, 40 (1) , 111-117. https://doi.org/10.1016/S0008-6215(00)82673-7
    46. J. Roth, K. Thoss, M. Wagner, H. W. Meyer. Electron microscopic demonstration of cell surface carbohydrates by means of peroxidase and ferritin complexes of the Lens culinaris lection. Histochemistry 1975, 43 (3) , 275-282. https://doi.org/10.1007/BF00499709
    47. J. Roth, K. Thoss. The use of fluorescein isothiocyanate-labelled lectins for immunohistological demonstration of saccharides. Experimentelle Pathologie 1975, 10 (5-6) , 258-267. https://doi.org/10.1016/S0014-4908(75)80032-9
    48. J. Roth, G. Neupert, K. Thoss. Interaction of Lens culinaris lectin, Concanavalin A, Ricinus communis agglutinin and wheat germ agglutinin with the cell surface of normal and transformed rat liver cells. Experimentelle Pathologie 1975, 10 (5-6) , 309-317. https://doi.org/10.1016/S0014-4908(75)80039-1
    49. J. Roth. Lens culinaris lectin receptors in the plasma membrane of rat liver cells: comparative electron microscopic studies on normal cells, on cells in vivo transformed by diethylnitrosamine and on Zajdela ascites hepatoma cells. Experimentelle Pathologie 1975, 11 (3-4) , 123-132. https://doi.org/10.1016/S0014-4908(75)80052-4
    50. K. Thoss, J. Roth. The use of fluorescein isothiocyanate labelled lectins for immunohistochemical demonstration of saccharides. Experimentelle Pathologie 1975, 11 (3-4) , 155-161. https://doi.org/10.1016/S0014-4908(75)80056-1
    51. J. Roth, K. Thoss. Light and electron microscopic demonstration ofd-mannose andd-glucose like sites at the cell surface by means of the lectin from theLens culinaris. Experientia 1974, 30 (4) , 414-414. https://doi.org/10.1007/BF01921694
    52. Annette M.C. Rapin, Max M. Burger. Tumor Cell Surfaces: General Alterations Detected by Agglutinins. 1974, 1-91. https://doi.org/10.1016/S0065-230X(08)60108-6
    53. Garth L. Nicolson. The Interactions of Lectins with Animal Cell Surfaces. 1974, 89-190. https://doi.org/10.1016/S0074-7696(08)60939-0
    54. M. Kohoutová, J. Kocourek. Mechanism of binding of the competence substance to the cell wall receptor sites. Folia Microbiologica 1973, 18 (6) , 506-513. https://doi.org/10.1007/BF02876798
    55. Donald M. Kirschenbaum. Molar absorptivity and A1cm1% values for proteins at selected wavelengths of the ultraviolet and visible regions. IX. Analytical Biochemistry 1973, 56 (1) , 237-263. https://doi.org/10.1016/0003-2697(73)90186-3
    56. Joel H. Shaper, Robert Barker, Robert L. Hill. Purification of wheat germ agglutinin by affinity chromatography. Analytical Biochemistry 1973, 53 (2) , 564-570. https://doi.org/10.1016/0003-2697(73)90107-3
    57. C. Borek, M. Grob, M.M. Burger. Surface alterations in transformed epithelial and fibroblastic cells in culture: A disturbance of membrane degradation versus biosynthesis?. Experimental Cell Research 1973, 77 (1-2) , 207-215. https://doi.org/10.1016/0014-4827(73)90569-7
    58. R. S. Turner, M. M. Burger. The cell surface in cell interactions. 1973, 121-155. https://doi.org/10.1007/3-540-06238-6_6
    59. M.D. Stein, H.J. Sage, M.A. Leon. Studies on a phytohemagglutinin from the common lentil. Experimental Cell Research 1972, 75 (2) , 475-482. https://doi.org/10.1016/0014-4827(72)90455-7
    60. Nathan Sharon, Halina Lis. Lectins: Cell-Agglutinating and Sugar-Specific Proteins. Science 1972, 177 (4053) , 949-959. https://doi.org/10.1126/science.177.4053.949
    61. Melvyn Greaves, George Janossy. Elicitation of Selective T and B Lymphocyte Responses by Cell Surface Binding Ligands. Immunological Reviews 1972, 11 (1) , 87-130. https://doi.org/10.1111/j.1600-065X.1972.tb00047.x
    62. Marshall D. Stein, Harvey J. Sage, M.A. Leon. Studies on a phytohemagglutinin from the lentil. Archives of Biochemistry and Biophysics 1972, 150 (2) , 412-420. https://doi.org/10.1016/0003-9861(72)90057-4
    63. Nancy Lewis Baenziger, G.N. Brodie, Philip W. Majerus. Isolation and Properties of a Thrombin-sensitive Protein of Human Platelets. Journal of Biological Chemistry 1972, 247 (9) , 2723-2731. https://doi.org/10.1016/S0021-9258(19)45271-X
    64. Irngard K. Howard, Harvey J. Sage, Curley B. Horton. Studies on the appearance and location of hemagglutinins from a common lentil during the life cycle of the plant. Archives of Biochemistry and Biophysics 1972, 149 (1) , 323-326. https://doi.org/10.1016/0003-9861(72)90328-1
    65. Harvey J. Sage, Robert W. Green. [38] Common lentil (Lens culinaris) phytohemagglutinin. 1972, 332-339. https://doi.org/10.1016/0076-6879(72)28040-5
    66. Stuart Kornfeld, John Rogers, Walter Gregory. The Nature of the Cell Surface Receptor Site for Lens culinaris Phytohemagglutinin. Journal of Biological Chemistry 1971, 246 (21) , 6581-6586. https://doi.org/10.1016/S0021-9258(19)34153-5
    67. Marshall D. Stein, Irmgard K. Howard, Harvey J. Sage. Studies on a phytohemagglutinin from the lentil. Archives of Biochemistry and Biophysics 1971, 146 (1) , 353-355. https://doi.org/10.1016/S0003-9861(71)80074-7
    68. Irmgard K. Howard, Harvey J. Sage, Marshall D. Stein, N. Martin Young, Myron A. Leon, Douglas F. Dyckes. Studies on a Phytohemagglutinin from the Lentil. Journal of Biological Chemistry 1971, 246 (6) , 1590-1595. https://doi.org/10.1016/S0021-9258(18)62353-1
    69. N. Martin Young, Myron A. Leon, Terumi Takahashi, Irmgard K. Howard, Harvey J. Sage. Studies on a Phytohemagglutinin from the Lentil. Journal of Biological Chemistry 1971, 246 (6) , 1596-1601. https://doi.org/10.1016/S0021-9258(18)62354-3
    70. Toshiaki SHINOHARA. Isolation and Properties of a Hemagglutinin from Seeds of Pisum sativum. Proceedings of the Japan Academy 1971, 47 (3) , 331-336. https://doi.org/10.2183/pjab1945.47.331
    71. Satoshi Toyoshima, Toshiaki Osawa, Akira Tonomura. Some properties of purified phytohemagglutinin from Lens culinaris seeds. Biochimica et Biophysica Acta (BBA) - Protein Structure 1970, 221 (3) , 514-521. https://doi.org/10.1016/0005-2795(70)90222-9
    72. G. Entlicher, J.V. Koštíř, J. Kocourek. Studies on phytohemagglutinins III. Isolation and characterization of hemagglutinins from the pea (Pisum sativum L.). Biochimica et Biophysica Acta (BBA) - Protein Structure 1970, 221 (2) , 272-281. https://doi.org/10.1016/0005-2795(70)90267-9
    73. M. Tichá, G. Entlicher, J.V. Koštíř, J. Kocourek. Studies on phytohemagglutinins. IV. Isolation and characterization of a hemagglutinin from the lentil, Lens esculenta, Moench. Biochimica et Biophysica Acta (BBA) - Protein Structure 1970, 221 (2) , 282-289. https://doi.org/10.1016/0005-2795(70)90268-0

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