Levine P, Katzin EM. Temporary agglutinability of red blood cells. Proc Soc Exp Biol NY 1938;39:167–9.10.3181/00379727-39-10133PSearch in Google Scholar
Hubener G. Untersuchungen uber isoagglutination mit besonderer berucksichtigung sheinarer abeweichungen von gruppenschema. Z Immun Forsch Allergie klin Immunol 1925;45:223–48.Search in Google Scholar
Thomsen O. Ein vermehrungsfahiges agens als veranderer des agglutinaorischen verhaltens der roten blutkorperchen, eine bisher unbekannte quelle der fehlbestimmung. Z Immun Forsch Allergie klin Immunol 1927;52:85–107.Search in Google Scholar
Friedenreich V. The Thomsen hemagglutination phenomenon. Copenhagen: Levine and Munksgaard, 1930.Search in Google Scholar
Judd WJ. Microbial forms of polyagglutination (T, Tk and acquired-B). In: Beck ML, Judd WJ, eds. Polyagglutination. Washington, DC: American Association of Blood Banks,
1980:23–53.Search in Google Scholar
Beck ML, Myers M, Moulds J, et al. Coexistent Tk and VA polyagglutination. Transfusion 1978; 18:680–4.10.1046/j.1537-2995.1978.18679077949.xSearch in Google Scholar
Sondag-Thull D, Levene NA, Levene C, et al. Characterization of a neuraminidase from Corynebacterium acquaticum responsible for Th polyagglutination. Vox Sang 1989; 57:193–8.10.1111/j.1423-0410.1989.tb00822.xSearch in Google Scholar
Judd WJ, McGuire-Mallory D, Anderson KM, et al. Concomitant T- and Tk-activation associated with acquired-B antigens. Transfusion 1979;29:293-7.
9-Thomas DB, Winzler RJ. Structural studies on human erythrocyte glycoproteins. Alkali-labile tetrasaccharides. J Biol Chem 1969;244:5943–6.Search in Google Scholar
Issitt PD. The MN blood group system. Cincinnati: Montgomery Scientific Publications; 1981.Search in Google Scholar
Bird GWG. Anti-T in peanuts. Vox Sang 1964;9:748–9.10.1111/j.1423-0410.1964.tb04072.xSearch in Google Scholar
Goldstein IJ, Hayes CE. The lectins: carbohydrate-binding proteins of plants and animals. In: Tipson RS, Horton D, eds. Adv Carbohydr Chem Biochem 1978;35:127–340.10.1016/S0065-2318(08)60220-6Search in Google Scholar
Bird GWG, Wingham J. Tk: a new form of polyagglutination. Br J Haematol 1972;23:759–63.10.1111/j.1365-2141.1972.tb03490.x4646828Search in Google Scholar
Inglis G, Bird GWG, Mitchell AAB, et al. Effect of Bacteroides fragtilis culture supemates on the human erythrocyte membrane: pathogenesis of Tk polyagglutination. J Clin Pathol 1975;28:964–8.10.1136/jcp.28.12.96447591354368Search in Google Scholar
Doinel C, Andreu G, Cartron JP, et al. Tk polyagglutination produced in vitro by an endo-β-galactosidase from Escherichia freundii. Vox Sang 1980;38:94–8.Search in Google Scholar
Judd WJ. The role of exo-ß-galactosidases in Tk-activation (abstract). Transfusion 1980;20:622.Search in Google Scholar
Inglis G, Bird GWG, Mitchell AAB, et al. Tk polyagglutination associated with reduced A and H reactivity. Vox Sang 1978;35:370–4.10.1111/j.1423-0410.1978.tb02949.x106548Search in Google Scholar
Andreu G, Doinel C, Cartron JP, et al. Induction of Tk polyagglutination by Bacteroides fragilis culture supemates: associated modifications of ABH and Ii antigens. Rev Fr Transfus Immunohematol l979;22:551–61.Search in Google Scholar
Gerbal A, Maslet C, Salmon Ch. Immunologic aspects of the acquired-B antigen. Vox Sang 1975;28:398—403.10.1111/j.1423-0410.1975.tb02787.x235812Search in Google Scholar
Garratty G, Willbanks E, Petz LD. Acquired-B antigen associated with Proteus mirabilis infection. Vox Sang 1971; 21:45–56.10.1111/j.1423-0410.1971.tb00556.x5120100Search in Google Scholar
Bird GWG, Wingham J, Beck ML, et al. Th, a “new” form of polyagglutination. Lancet 1978;i: 1215–6.10.1016/S0140-6736(78)91013-9Search in Google Scholar
Bird GWG. Lectins and red cell polyagglutination: history, comments and recent developments. In: Beck ML, Judd WJ, eds. Polyagglutination. Washington, DC: American Association of Blood Banks, 1980:71-90.Search in Google Scholar
Bird GWG, Wingham J, Seger R, Kenny AB. Tx, a “new” red cell cryptantigen exposed by pneumococcal enzymes. Blood transfus and immunohematol 1982;25:215–6.10.1016/S0338-4535(82)80009-3Search in Google Scholar
Wolach B, Sadan N, Bird GWG, et al. Tx polyagglutination in three members of one family. Acta Haematol 1987;78:45–7.10.1159/000205835Search in Google Scholar
Bird GWG, Shinton NK, Wingham J. Permanent mixed-field polyagglutination. Br J Haematol 1971;21:443–53.10.1111/j.1365-2141.1971.tb02705.xSearch in Google Scholar
Beck ML. Tn: a nonmicrobial form of polyagglutination. In: Beck ML, Judd WJ, eds. Polyagglutination. Washington, DC: American Association of Blood Banks, 1980:55–70.Search in Google Scholar
Berman HJ, Smarto J, Issitt CH, Issitt PD, Marsh WL, Jensen L. Tn-activation with acquired A-like antigen. Transfusion 1972;12:35–45.10.1111/j.1537-2995.1972.tb00020.xSearch in Google Scholar
Bird GWG, Wingham J, Pippard MJ, et al. Erythrocyte membrane modification in malignant diseases of myeloid and lym-phoreticular tissues. I. Tn-polyagglutination in myelocytic leukemia. Br J Haematol 1976;33:289–94.10.1111/j.1365-2141.1976.tb03540.xSearch in Google Scholar
Ness PM, Garratty G, Morel PA, Perkins HA. Tn polyagglutination preceding acute leukemia. Blood 1979;54:30–4.10.1182/blood.V54.1.30.30Search in Google Scholar
Bird GWG, Wingham J, Richardson SGN. Myelofibrosis, autoimmune hemolytic anemia and Tn polyagglutinability. Haematologia 1985; 18:99-104.
31-Janvier D, Guigner F, Reviron M, Benbunan M. Concomitant exposure of Th and Tn cryptantigens on the red cells of a patient with myelodysplasia. Vox Sang 1991;61:142–3.10.1111/j.1423-0410.1991.tb00263.xSearch in Google Scholar
Cartron JP, Cartron J, Andreu G, et al. Selective deficiency of 3-β·galactosyl-transferase (T-transferase) in Tn-polyagglutin-able erythrocytes. Lancet 1978;i:856–7.10.1016/S0140-6736(78)90197-6Search in Google Scholar
Dahr W, Uhlenbruck G, Bird GWG. Cryptic A-like receptor sites in human erythrocyte glycoproteins: proposed nature of Tn-antigen. Vox Sang 1974;27:29–42.10.1111/j.1423-0410.1974.tb02386.x4368542Search in Google Scholar
Wilson MJ, Cott ME, Sotus PE. Probable Tn-activation in utero (abstract). Transfusion 1980;20:622.Search in Google Scholar
Rose RR, Skradski KJ, Polesky HF, et al. Transient neonatal Tn-activation: another example (abstract). Transfusion 1983; 23:422.Search in Google Scholar
Schulz M, Fortes P, Brewer L, et al. “In utero” exposure of Tn and Th cryptantigens (abstract). Transfusion l983;23:422.Search in Google Scholar
Wahl CM, Herman JH, Shirey RS, et al. Th activation of maternal and cord blood. Transfusion 1989;29:635-7.10.1046/j.1537-2995.1989.29789369684.xSearch in Google Scholar
Race RR, Sanger R. Blood groups in man. 6th ed. Oxford: Blackwell Scientific Publications, 1975.Search in Google Scholar
Herman JH, Shirey RS, Smith B, Kidder TS, Ness PM. Th activation in congenital hypoplastic anemia. Transfusion 1987;27:253–6.10.1046/j.1537-2995.1987.27387235633.xSearch in Google Scholar
Cazal P, Monis M, CaubelJ, et al. Polyagglutinabilité héredi-taire dominante: antigen privé (Cad) correspondent à un anticorps public et à une lectine de Dolicbos biflorus. Rev Fr Transfus Immunohematol 1968;11:209–21.10.1016/S0035-2977(68)80050-1Search in Google Scholar
Gerbal A, Lopez M, Maslet C, et al. Polyagglutinability associated with the Cad antigen. Hematologia 1976;10:383–91.Search in Google Scholar
Cazal P, Monis M, Bizot M. Les antigènes Cad en 1976. Rev Fr Transfus Immunohematol 1977;20:165–73.10.1016/S0338-4535(77)80031-7Search in Google Scholar
Sanger R, Gavin J, Tippett P, et al. Plant agglutinin for another human blood group. Lancet 1971;i:1130.10.1016/S0140-6736(71)91865-4Search in Google Scholar
Lewis M, Kaita H, Chown B, et al. A family with the rare red cell antigens Wra and “super” Sda. Vox Sang 1973;25:336–40.Search in Google Scholar
Tippett P, Gavin J, Bird GWG, Wingham J. Cad (Super Sda) in a British family with eastern connections: a note on the specificity of the Dolicbos biflorus lectin. J Immunogenet 1976;3:297–302.10.1111/j.1744-313X.1976.tb00587.xSearch in Google Scholar
Blanchard D, Cartron JP, Fournet B, et al. Primary structure of the oligosaccharide determinant of blood group Cad specificity. J Biol Chem 1983;258:7691–5.10.1016/S0021-9258(18)32234-8Search in Google Scholar
Herkt F, Parente JP, Leroy Y, et al. Structure determinations of the oligosaccharides isolated from Cad erythrocyte membranes by permethylation analysis and 500-MHZJH-NMR spectroscopy. EurJBiochem 1985;146:125–9.Search in Google Scholar
Donald ASR, Yates AD, Soh CPC, et al. A blood group Sda-active pentasaccharide isolated from Tamm-Horsfall urinary glycoprotein. Biochem Biophys Res Comm 1983;115:625–31.10.1016/S0006-291X(83)80190-9Search in Google Scholar
Donald ASR, Yates AD, Soh CPC, et al. The human blood group Sda determinant: a terminal non-reducing carbohydrate structure in TV-linked and mucin-type glycoproteins. Biochem Soc Trans 1984;12:596-9.10.1042/bst01205966208063Search in Google Scholar
Issitt PD. The antigens Sda and Cad. In: Moulds JM, Woods LL, eds. Blood groups P, I, Sda and Pr. Arlington, VA: American Association of Blood Banks, 1991:53–71.Search in Google Scholar
Harris PA, Roman GK, Moulds JJ, et al. An inherited RBC characteristic, Nor, resulting in erythrocyte polyagglutination. Vox Sang 1982;42:134–40.10.1111/j.1423-0410.1982.tb01083.x7072192Search in Google Scholar
Crookston JH, Crookston MC, Bumie KL, et al. Hereditary erythroblastic multinuclearity with a positive acidified serum test: a type of congenital dyserythropoietic anemia. Br J Haematol 1969;17:11–26.10.1111/j.1365-2141.1969.tb05660.xSearch in Google Scholar
Crookston JH, Crookston MC, Rosse WF. Red cell abnormalities in HEMPAS (hereditary erythroblastic multinuclearity with a positive acidified serum test). Br J Haematol 1972;23:83–91.10.1111/j.1365-2141.1972.tb03507.xSearch in Google Scholar
Gockerman JP, Durocher JR, Conrad ME. The abnormal surface characteristics of the red blood cell membrane in congenital dyserythropoietic anemia type II (HEMPAS). Br J Haematol 1975;30:383–94.10.1111/j.1365-2141.1975.tb01852.xSearch in Google Scholar
Graninger W, Rameiss H, Fisher K, et al. “VA”: a new type of erythrocyte polyagglutination characterized by depressed H receptors and associated with hemolytic anemia. I. Serological and hematological observations. Vox Sang 1977;32:195–200.Search in Google Scholar
Graninger W, Poschmann A, Fisher K, et al. “VA”: a new type of erythrocyte polyagglutination characterized by depressed H receptors and associated with hemolytic anemia. II. Observations by immunofluorescence, electron microscopy, cell electrophoresis and biochemistry. Vox Sang 1977; 32:201-7.10.1111/j.1423-0410.1977.tb00630.xSearch in Google Scholar
Bird AR, Kent P, Moores PP, Elliott T. Haemoglobin M-Hyde Park associated with polyagglutinable red cells in a South African family. Br J Haematol 1988;68:459–64.10.1111/j.1365-2141.1988.tb04236.xSearch in Google Scholar
King MJ, LiewYW, Moores PP, Bird GWG. Enhanced reaction with Vicia graminea lectin and exposed 7V-acetylglu-cosaminyl residues on a sample of human red cells with Hb M-Hyde Park. Transfusion 1988;28:549-–55.10.1046/j.1537-2995.1988.28689059029.xSearch in Google Scholar
Fukuda M, Dell A, Oates JE, Fukuda MN. Structure of branched lactosaminoglycan, the carbohydrate moiety of Band 3 isolated from adult human erythrocytes. J Biol Chem 1984;259:2860–73.10.1016/S0021-9258(17)39722-3Search in Google Scholar
Beck ML, Hicklin B, Pierce SR. Unexpected limitations in the use of commercial antiglobulin reagents. Transfusion 1976;16:71–5.10.1046/j.1537-2995.1976.16176130839.x1082669Search in Google Scholar
Buskila D, Levene C, Bird GW, Levene NA. Polyagglutination in hospitalized patients: a prospective study. Vox Sang 1987;52:99–102.10.1111/j.1423-0410.1987.tb03000.x3496714Search in Google Scholar
Judd WJ, Beck ML, Hicklin BL, Iyer PN, Goldstein IJ. BS II lectin: a second hemagglutinin isolated from Bandeiraea simplicifolia seeds with affinity for type III polyagglutinable red cells. Vox Sang 1977;33:246-51.Search in Google Scholar
Gray JM, Beck ML, Oberman HA. Clostridial-induced type I polyagglutinability with associated intravascular hemolysis. Vox Sang 1972;22:379–83.10.1111/j.1423-0410.1972.tb03984.x5020144Search in Google Scholar
Judd WJ. Oberman HA, Flynn S. Fatal intravascular hemolysis associated with T-polyagglutination. Transfusion 1982;22: 345–6.10.1046/j.1537-2995.1982.22482251231.x6285558Search in Google Scholar
Levene C, Sela R, Blat J, et al. Intravascular hemolysis aggravated by transfusion with fresh whole blood and renal failure in a palient wilh T polyagglutination. Transfusion 1986;26: 243–5.10.1046/j.1537-2995.1986.26386209379.x3705141Search in Google Scholar
Levene NA, Levene C, Gekker K, et al. Th polyagglutination with fatal outcome in a patient with massive hemolysis and perforated tumor of the colon. Am J Hematol 1990;35:127–8.10.1002/ajh.28303502132399903Search in Google Scholar
van Loghem JJ Jr, van der Hart M, Land ME. Polyagglutinability of red cells as a cause of severe hemolytic transfusion reactions. Vox Sang 1955;5:125–8.Search in Google Scholar
Heddle NM, Blajchman MA, Bodner N, et al. Absence of hemolysis of T-activated red cells following transfusion of blood products (abstract). Transfusion 1978; 18:384.Search in Google Scholar
Seger R, Joller P, Bird GWG, et al. Necrotising enterocolitis and neuraminidase-producing bacteria. Pediatr Acta 1981;35:121–8.Search in Google Scholar
Seger R, Joller P, Baerlocher K, et al. Hemolytic-uremic syndrome associated with neuraminidase-producing microorganisms: treatment by exchange transfusion. Helv Paediatr Acta 1980;35:359–67.Search in Google Scholar
Anglin JH Jr, Lemer MP, Nordquist RE. Blood group-like activity released by human mammary carcinoma cells in culture. Nature 1977;269:254–5.10.1038/269254a0593323Search in Google Scholar
Lloyd RV, Foley J, Judd WJ. Peanut lectin agglutinin and α-lac-talbumin: binding and immunohistochemical localization in breast tissues. Arch Pathol Lab Med 1984;108:392–5.Search in Google Scholar
Springer GF, Murthy MS, Desai PR, et al. Human carcinoma associated Thomsen-Freidenreich (T) antigens and the host’s immune response to it. In: Proteins of biological fluids, 27th Colloquium, 1979-Oxford: Pergamon Press, 1980:211–6.Search in Google Scholar
Reading CL, Bator J, O’Kennedy R. Monoclonal antibodies in tumor therapy. In: Moulds JM, Masouredis SP, eds. Monoclonal antibodies. Arlington, VA: American Association of Blood Banks, 1989:145–79.Search in Google Scholar
Judd WJ. Methods in immunohematology. Miami: Montgomery Scientific Publications, 1988.Search in Google Scholar
Judd WJ. The use of purified lectins in immunohematology. Transfusion l979;29:768-9.Search in Google Scholar
Aminoff D. Methods for the quantitative estimation of /V-acetylneuraminic acid and their applications to hydrolysates of sialmucoids. BiochemJ 1961;81:384—92.Search in Google Scholar
Bangham AD, Piemans R, Heard DH, Seaman GVF. An apparatus for microelectrophoresis of small particles. Nature 1958;183:642–4.10.1038/182642a013590051Search in Google Scholar
van Oss CJ, Mohn JF, Cunningham RK. Physicochemical aspects of hemagglutination. In: Mohn JF, Plunkett RW, Cunningham RK, eds. Human blood groups. Basel: Karger 1974:56–64.Search in Google Scholar
van Oss CJ, Mohn JF, Cunningham RK. Influence of various physicochemical factors on hemagglutination. Vox Sang 1978;34:351–61.10.1159/000467620Search in Google Scholar
Anstee DJ. The blood group MNSs-active sialoglycoproteins. Semin Haematol 1981;18:13–31.Search in Google Scholar
