Portal de Periódicos da CAPES

INTRODUCTION: IMMUNOCHEMISTRY OF ENZYMES

1963; Wiley; Volume: 103; Issue: 2 Linguagem: Inglês

10.1111/j.1749-6632.1963.tb53717.x

1749-6632

B. Cinader,

Advanced biosensing and bioanalysis techniques

Annals of the New York Academy of SciencesVolume 103, Issue 2 p. 495-548 INTRODUCTION: IMMUNOCHEMISTRY OF ENZYMES B. Cinader, B. Cinader Subdivision of Immunochemistry, Division of Biological Research, Ontario Cancer Institute, and Departments of Medical Biophysics and Pathological Chemistry, University of Toronto, Toronto, CanadaSearch for more papers by this author B. Cinader, B. Cinader Subdivision of Immunochemistry, Division of Biological Research, Ontario Cancer Institute, and Departments of Medical Biophysics and Pathological Chemistry, University of Toronto, Toronto, CanadaSearch for more papers by this author First published: May 1963 https://doi.org/10.1111/j.1749-6632.1963.tb53717.xCitations: 71AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 Ackermann, W. W. & V. R. Potter. 1949. Enzyme inhibition in relation to chemotherapy. Proc. Soc. Exptl. Biol. Med. 72: 1–9. 1a Adams, M. H. 1942. Reaction between the enzyme tyrosinase and its specific antibody. J. Exptl. Med. 76: 175–184. 2 Aksoy, M. 1955. Anti-hemoglobin serum production and its relationship to fetal and adult hemoglobin. Acta. Haematol. 13: 226–234. 3 Alberty, R. A. 1956. Enzyme kinetics. Advan. Enzymol. 17: 1–64. 4 Allen, P. Z. & E. A. Kabat. 1957. Studies on the capacity of some polysaccharides to elicit antibody formation in man. J. Exptl. Med. 105: 383–394. 5 Allison, A. C. 1959. Genetic control of human haptoglobin synthesis. Nature. 183: 1312–1314. 6 Allison, A. C. & B. S. Blumberg. 1961. An iso-precipitation reaction distinguishing human serum-protein types. Lancet. 1: 634–637. 7 Amano, T., H. Fujio, S. Kishiguchi, Y. Noma, S. Shinka & Y. Saiki. 1956. The antigenicity of crystalline taka-amylase A. Med. J. Osaka Univ. 7: 593–602. 8 Amos, D. B. 1962. Isoantigens of mouse red cells. Ann. N. Y. Acad. Sci. 97: 69–82. 9 Anderson, P. J., S. Cohen & T. Barka. 1961. Hepatic injury. A histochemical study of intracytoplasmic globules occurring in liver injury. Arch. Pathol. 71: 89–95. 9a Antoni, F. & T. Keleti. 1957. Immune-biological study of the crystalline alcohol dehydrogenases isolated from closely related yeast species. Acta. Physiol. Acad. Sci. Hung. 13: 187–197. 10 Appella, E. & C. L. Markert. 1961. Dissociation of lactate dehydrogenase into subunits with guanidine hydrochloride. Biochem. Biophys. Res. Commun. 6: 171–176. 11 Arends, T. & M. L. G. de Rodriguez. 1960. Haptoglobin in monkeys. Nature. 185: 325–326. 12 Aschaffenburg, R. & J. Drewry. 1955. Occurrence of different beta-lacto-globulins in cow's milk. Nature. 176: 218–219. 13 Aschaffenburg, R. & J. Drewry. 1957. Genetics of the beta-lactoglobulins in cow's milk. Nature. 180: 376–378. 14 Ashton, G. C. 1958. A genetic mechanism for "thread protein" polymorphism in cattle. Nature. 182: 65–66. 15 Ashton, G. C. & E. I. McDougall. 1958. Beta-globulin polymorphism in cattle, sheep and goats. Nature. 182: 945–946. 16 Ashton, G. C. 1958. Further β-globulin phenotypes in sheep. Nature. 182: 1101–1102. 17 Ashton, G. C. 1958. Genetics of beta-globulin polymorphism in British cattle. Nature. 182: 370–472. 18 Ashton, G. C. 1959. β-globulin alleles in some zebu cattle. Nature. 184: 1135–1136. 19 Ashton, G. C. 1960. Thread protein and β-globulin polymorphism in the serum proteins of pigs. Nature. 186: 991–992. 20 Babson, A. L. & T. Winnick. 1954. Protein transfer in tumor-bearing rats. Cancer Research. 14: 606–611. 21 Bach, M. L., E. R. Signer, C. Levinthal & I. W. Sizer. 1961. The electrophoretic patterns of alkaline phosphatase from various E. coli mutants. Federation Proc. 20: 255. 22 Bangham, A. D. 1957. Distribution of electrophoretically different haemoglobins among cattle breeds of Great Britain. Nature. 179: 467–468. 23 Bearn, A. G. & E. C. Franklin. 1958. Some genetical implications of physical studies of human haptoglobins. Science. 128: 596–597. 24 Bearn, A. G. & E. C. Franklin. 1959. Comparative studies on the physical characteristics of the heritable haptoglobin groups of human serum. J. Exptl. Med. 109: 55–68. 25 Beckman, L. 1959. Atypical haptoglobin patterns in tumor patients. Lancet. 2: 952–953. 26 Beckman, L. & G. Cedermark. 1960. Haptoglobin types in Macaca irus. Nature. 186: 643–644. 27 Benacerraf, B. & P. G. H. Gell. 1961. Delayed hypersensitivity to homologous γ-globulin in the guinea pig. Nature. 189: 586–587. 28 Berson, S. A. & R. S. Yalow. 1961. Immunochemical distinction between insulins with identical amino-acid sequences. Nature. 191: 1392–1393. 29 Billingham, R. E., L. Brent & P. B. Medawar. 1953. 'Actively acquired tolerance' of foreign cells. Nature. 172: 603–606. 30 Billingham, R. E., L. Brent & P. B. Medawar. 1955. Acquired tolerance of skin homografts. Ann. N. Y. Acad. Sci. 59: 409–416. 31 Billingham, R. E., L. Brent & P. B. Medawar. 1956. Quantitative studies on tissue transplantation immunity. III. Actively acquired tolerance. Phil. Trans. Roy. Soc. London Ser. B. 239: 357–414. 32 Blumberg, B. S. Personal communication. 33 Blumberg, B. S. 1960. Biochemical polymorphisms in animals: haptoglobins and transferrins. Proc. Soc. Exptl. Biol. Med. 104: 25–28. 34 Blumberg, B. S., A. C. Allison & B. Garry. 1960. The haptoglobins, hemoglobins and serum proteins of the Alaskan Fur Seal, Ground Squirrel and Marmot. J. Cellular Comp. Physiol. 55: 61–71. 35 Blumberg, B. S., S. Dray & J. C. Robinson. 1962. Antigen polymorphism of a low-density β lipoprotein. Allotypy in human serum. Nature. 194: 656–658. 36 Blumberg, B. S. & J. Robbins. 1960. Thyroxine-serum protein complexes: single dimension gel and paper electrophoresis studies. Endocrinology. 67: 368–378. 37 Blumberg, B. S. & M. P. Tombs. 1958. Possible polymorphism of bovine α-lact-albumin. Nature. 181: 683–684. 38 Bollet, A. J., J. S. Davis & J. O. Hurt. 1962. Lack of species specificity of antibody to an enzyme. J. Exptl. Med. 116: 109–118. 39 Boyer, P. D. & A. R. Schulz. 1959. Some aspects of protein structure in relation to the role of -SH and -S-S- groups in enzymic catalysis. In Sulfur in Proteins. R. Benesch, Ed. Academic Press. New York . Pp. 199–213. 40 Boyer, S. H. & W. J. Young. 1960. β-globulin polymorphism in Chimpanzees. Nature. 187: 1035–1036. 41 Brambell, F. W. R. 1961. The transmission of antibodies from mother to foetus. Proc. Roy. Soc. Med. 54: 992–993. 42 Brambell, F. W. R., R. Hallday & W. A. Hemmings. 1961. Changes in 131I-labelled immune bovine γ-globulin during transmission to the circulation after oral administration to the young rat. Proc. Roy. Soc. London. Ser. B. 153: 477–489. 43 Brambell, F. W. R., W. A. Hemmings & M. Henderson. 1951. Antibodies and Embryos. Univ. London, Athlone Press. London . 44 Branster, M. & B. Cinader. 1961. The interaction between bovine ribonuclease and antibody: a study of the mechanism of enzyme inhibition by antibody. J. Immunol. 87: 18–38. 45 Brenner, S. & R. W. Horne. 1959. A negative staining method for high resolution electron microscopy of viruses. Biochim. Biophys. Acta. 34: 103–110. 46 Brenner, S., F. Jacob & M. Meselson. 1961. An unstable intermediate carrying information from genes to ribosomes for protein synthesis. Nature. 190: 576–581. 47 Brönnestam, R. & S. B. Nilsson. 1957. Gamma-globulin groups (Gm) of mothers and their newborn infants. Vox Sanguinis. 2: 316–319. 48 Brown, R. K. 1963. Immunologic studies of bovine ribonuclease derivatives. Ann. N. Y. Acad. Sci. 103 (2): 754–764. 49 Brown, R. K., R. Delaney, L. Levine & H. Van Vunakis. 1959. Studies on the antigenic structure of ribonuclease. I. General role of hydrogen and disulfide bonds. J. Biol. Chem. 234: 2043–2049. 50 Bueding, E. & J. MacKinnon. 1955. Studies of the phosphoglucose isomerase of schistosoma mansoni. J. Biol. Chem. 215: 507–513. 51 Busch, H., E. Fujiwara & D. C. Firszt. 1961. Studies on the metabolism of radioactive albumin in tumor-bearing rats. Cancer Research. 21: 371–377. 52 Bussard, A. 1957. Tolérance immunologique provoquée chez le Lapin envers certains antigènes de la levure. Compt. Rend. 245: 2430–2433. 53 Cabannes, R. & C. Serain. 1955. Étude de l'hémoglobine du dromadaire d'Afrique du Nord. Compt. Rend. Soc. Biol. 149: 1103–1105. 54 Cahn, R. D., N. O. Kaplan, L. Levine & L. E. Zwlling. 1962. Nature and development of lactic dehydrogenases. Science 136: 962–969. 55 Campbell, D. H. & L. Fourt. 1939. Immunochemistry of catalase. J. Biol. Chem. 129: 385–392. 56 Carter, B. G. & B. Cinader. 1960. Some experiments on acquired immunological tolerance in the goat. Ann. N. Y. Acad. Sci. 87: 36–79. 57 Carter, B. G., B. Cinader & C. A. Ross. 1961. Immunochemical analysis of the multiple forms of bovine ribonuclease. Ann. N. Y. Acad. Sci. 94: 1004–1029. 58 Cebra, J. J. 1961. Studies on the combining sites of the protein antigen silk fibroin. I. Characterization of the fibroin-rabbit antifibroin system. J. Immunol. 86: 190–196. 59 Cebra, J. J. 1961. Studies on the combining sites of the protein antigen silk fibroin. III. Inhibition of the silk fibroin-antifibroin system by peptides derived from the antigen. J. Immunol. 86: 205–214. 60 Cebra, J. J. 1961. Studies on the combining sites of the protein antigen silk fibroin. II. Isolation and characterization of peptides from chymotryptic hydrolysate of silk fibroin (Bombyx mori). J. Immunol. 86: 197–204. 61 Chase, M. W. 1959. Immunologic tolerance. Ann. Rev. Microbiol. 13: 349–376. 62 Chernoff, A. I. 1953. Immunologic studies of hemoglobins. II. Quantitative precipitin test using anti fetal hemoglobin sera. Blood. 8: 413–421. 63 Cinader, B. 1953. Antigen-antibody interaction using enzymes as antigens. Biochem. Soc. Symp. Cambridge England. 10: 16–36. 64 Cinader, B. 1955. Étude de la réaction enzyme-antienzyme. Bull. Soc. Chim. Biol. 37: 761–781. 65 Cinader, B. 1957. Antibodies against enzymes. Ann. Rev. Microbiol. 11: 371–390. 66 Cinader, B. 1957. The Danysz effect: an investigation of the reaction between an enzyme and its antibody. Brit. J. Exptl. Pathol. 38: 362–376. 67 Cinader, B. 1958. The Danysz effect and the lattice hypothesis. Abstr. 7th Int. Congr. Microbiol. Stockholm , Sweden . 68 Cinader, B.. 1960. Specificity and inheritance of antibody response: a possible steering mechanism. Nature. 188: 619–622. 69 Cinader, B. 1961. Quelques aspects de la tolérance immunologique à l'égard d'antigènes définis. Ann. Inst. Pasteur. 100: 265–289. 70 Cinader, B. 1962. Acquired tolerance, autoantibodies and cancer. Can. Med. Assoc. J., 86: 1161–1165. 71 Cinader, B. 1963. Perspectives and prospects of immunotherapy. Auto-antibodies and acquired immunological tolerance. In Canad. Cancer Conf. 5: 279–318. Academic Press. New York and London . 72 Cinader, B. & M. Branster. 1961. Antibody to ribonuclease—a study of the mechanism of enzyme inhibition by antibody. Paper presented at the 5th International Congress of Biochemistry, Moscow . In press. 73 Cinader, B. & J. M. Dubert. 1955. Acquired immune tolerance to human albumin and response to subsequent injections of diazo human albumin. Brit. J. Exptl. Pathol. 36: 515–529. 74 Cinader, B. & J. M. Dubert. 1956. Specific inhibition of response to purified protein antigens. Proc. Roy. Soc. London Ser. B. 146: 18–33. 75 Cinader, B. & S. Dubiski. 1963. The effect on immunogenicity of acquired immunological tolerance. In Colloque sin la Tolérance Acquise et la Tolérance Naturelle à l'Égard de Substances Antigèniques Définies. Pp. 255–305. Edition du Centre Natl. Rech. Sci. Paris . 76 Cinader, B. & J. H. Pearce. 1956. Immunochemical studies on bovine ribonuclease. Brit. J. Exptl. Pathol. 37: 541–552. 77 Cinader, B. & J. H. Pearce. 1958. Immunological approaches to the study of ribonuclease. In Symposium on Protein Structure. Pp. 240–246. A. Neuberger, Ed. Methuen. London , England . 78 Cinader, B. & J. H. Pearce. 1958. The specificity of acquired immunological tolerance to azo proteins. Brit. J. Exptl. Pathol. 39: 8–29. 79 Cinader, B., J. H. Pearce & B. G. Carter. 1958. Acquired immunological tolerance to bovine ribonuclease. Nature. 181: 1208–1209. 80 Cinader, B. & B. Weitz. 1953. Interaction of tetanus toxin and antitoxin. J. Hyg. 51: 293–310. 81 Cleve, H., B. Ramot & A. G. Bearn. 1962. Distribution of serum group-specific components in Israel. Nature. 195: 86–87. 82 Cohen, G. N. & R. Munier. 1959. Effets des analogues structuraux d'amino acides sur la croissance, la synthèse de protéines et la synthèse d'enzymes chez Escherichia Coli. Biochim. Biophys. Acta. 31: 347–356. 83 Cohen, P. P. & G. W. Brown. 1960. Ammonia metabolism and urea biosynthesis. In Comparative Biochemistry. 2: 161–244. M. Florkin, Ed. Academic Press, New York . 84 Cohen, S., M. Beiser & K. C. Hsu. 1961. Immunohistochemical study of the uptake of serum proteins by neoplastic liver cells. Cancer Research. 21: 1510–1512. 85 Cohn, M. & J. Monod. 1951. Purification et propriétés de la β-galactosidase (lactose) d'Escherichia coli. Biochim. Biophys. Acta. 7: 153–174. 86 Cohn, M. & A. M. Torriani. 1952. Immunochemical studies with the β-galactosidase and structurally related protein of Escherichia coli. J. Immunol. 69: 471–491. 87 Cohn, M. & A. M. Torriani. 1953. The relationships in biosynthesis of the β-galactosidase and Pz-proteins in Eschetichia coli. Biochim. Biophys. Acta. 10: 280–289. 88 Colter, J. S., D. Kritchevsky, H. H. Bird & R. F. J. McCandless. 1957. In vitro studies with antisera against tumor cell protein fractions. Cancer Research. 17: 272–276. 89 Croisille, Y. 1962. Étude immuno-électrophorétiquc des estérases de foie de Poulet adulte et embryonnaire. Compt. Rend. 254: 2103–2105. 90 Croisille, Y. 1962. Les estérases du sérum de Poulet adulte et embryonnaire étudiées par la méthode d'analyse immuno-électrophorétique. Compt. Rend. 254: 253–2255. 91 Cumley, R. W. & M. R. Irwin. 1943. Individual specificity of human serum. J. Immunol. 46: 63–70. 92 Curtain, C. C. 1959. The use of acquired immunological tolerance and immunological "paralysis" in the study of the antigenic relationships of normal and abnormal serum globulins. Brit. J. Exptl. Pathol. 40: 255–262. 93 Deutsch, H. F. & A. Saebra. 1935. Immunochemical studies and assay of catalase. J. Biol. Chem. 214: 455–462. 94 Diamond, J. M. & G. Braunitzer. 1962. α-chain of rabbit haemoglobin. Nature. 194: 1287–1288. 95 Dixon, F. J. & P. H. Maurer. 1955. Immunologic unresponsiveness induced by protein antigens. J. Exptl. Med. 101: 245–257. 96 Dolby, D. E., D. A. Hall & F. C. Happold. 1952. The formation and structure of an adaptive enzyme, tryptophanase, and its specific anti-enzyme. Brit. J. Exptl. Pathol. 33: 304–314. 97 Dray, S. & G. O. Young. 1960. Genetic control of two γ-globulin isoantigenic sites in domestic rabbits. Science. 131: 738–739. 97a Dubiski, S. & B. Cinader. 1963. A new allotypic specificity in the mouse (MuA2). Nature. 197: 705. 98 Dubiski, S., A. Dubiska, D. Skalba & A. Kelus. 1961. Antigenic structure of rabbit γ-globulin. Immunology. 4: 236–243. 99 Dubiski, S., Z. Dudziak & D. Skalba. 1959. Serum groups in rabbits. Immunology 2: 84–92. 100 Earle, D. P., M. P. Hutt, K. Schmid & D. Gitlin. 1959. Observations on double albumin—a genetically transmitted serum protein anomaly. J. Clin. Invest. 38: 1412–1420. 100a Easton, J. M., B. Goldberg & H. Green. 1962. Demonstration of surface antigens and pinocytosis in mammalian cells with ferritin-antibody conjugates. J. Cell Biol. 12: 437–443. 101 Easton, J. M., B. Goldberg & H. Green. 1962. Immune cytolysis: electron microscope localization of cellular antigens with ferritin-antibody conjugates,. J. Exptl. Med. 115: 275–288. 102 Ellem, K. A. O. 1957. Studies on the mechanism of the cytotoxic action of antisera. Australian J. Sci. 20: 116–117. 103 Ellem, K. A. O. 1958. Some aspects of the ascites tumor cell response to a heterologous antiserum. Cancer Research. 18: 1179–1185. 104 Elödi, P. & H. Szabolcsi. 1959. Role of the coenzyme in the stabilization of glyceraldchyde-3-phosphate dehydrogenase. Nature. 184: 56. 105 Epstein, W. V. & H. Fudenberg. 1962. Demonstration of Gm 1 (a) and anti-Gm 1 (a) specificities by tanned cells coated with individual γ-globulins. J. Immunol. 89: 293–299. 106 Evans, J. V., J. W. B. King, B. L. Cohen, H. Harris & F. L. Warren. 1956. Genetics of haemoglobin and blood potassium differences in sheep. Nature. 178: 849–850. 107 Fazekas de St Groth, S.. Personal communication. 108 Freese, E. 1961. Paper presented at the 5th International Congress of Biochemistry, Moscow . In press. 108a Fujio, H., S. Kishicuchi, S. Shinka, Y. Saiki & T. Amano. 1959. Immunochemical studies on lysozyme. 1. Comparative studies of lysozyme and lysozyme methyl ester. Biken's J. 2: 56–76. 109 Gershowitz, H., R. D. Owen & N. H. Horowitz. Unpublished data. See reference 242. 110 Gessard, C. 1901. Études sur la tyrosinase. Ann. Inst. Pasteur. 15: 593–614. 111 Gessard, C. 1902. Tyrosinase et antityrosinase. Compt. Rend. Soc. Biol. 54: 551–553. 112 Giblett, E. R., C. G. Hickman & O. Smithies. 1959. Serum transferrins. Nature 183: 1589–1590. 113 Giblett, E. R. & A. G. Steinberg. 1960. The inheritance of serum haptoglobin types in American Negroes, evidence for a third allele Hp-2m. Am. J. Human Genet. 12: 160–169. 114 Glenny, A. T. & M. Barr. 1932. "Dilution ratio" of diphtheria antitoxin as a measure of avidity. J. Pathol. Bacteriol. 35: 91–96. 115 Goldstein, A. 1944. Mechanism of enzyme-inhibitor-substrate reactions. Cholinesterase-eserine-acetylcholine system. J. Gen. Physiol. 27: 529–580. 116 Goodman, M. & D. H. Campbell. 1953. Differences in antigenic specificity of human normal adult, fetal, and sickle cell anemia hemoglobin. Blood. 8: 422–433. 117 Gorer, P. A., S. Lyman & G. D. Snell. 1948. Studies on the genetic and antigenic basis of tumor transplantation. Linkage between a histocompatibility gene and "fused" in mice. Proc. Roy. Soc. London Ser. B. 135: 499–505. 118 Green, H., P. Barrow & B. Goldberg. 1959. Effect of antibody and complement on permeability control in ascites tumor cells and erythrocytes. J. Exptl. Med. 110: 699–713. 119 Green, H., R. A. Fleischer, P. Barrow & B. Goldberg. 1959. The cytotoxic action of immune gamma globulin and complement on Krebs ascites tumor cells. II. Chemical studies. J. Exptl. Med. 109: 511–521. 120 Gregory, K. F. & F. Wróblewski. 1958. Preparation and properties of purified antilactate dehydrogenase. J. Immunol. 81: 359–367. 121 Grubb, R. 1956. Agglutination of erythrocytes coated with "incomplete" anti-Rh by certain rheumatoid arthritic sera and some other sera; the existence of human serum groups. Acta. Pathol. Microbiol. Scand. 39: 195–197. 122 Grubb, R. & A. B. Laurell. 1956. Hereditary serological human serum groups. Acta. Pathol. Microbiol. Scand. 39: 390–398. 123 Grubb, R. 1957. A relationship between blood group serology and rheumatoid arthritis serology. Serum protein groups. Vox Sanguinis. 2: 305–312. 124 Grubb, R. 1958. Interactions between rheumatoid arthritic sera and human gamma-globulin. Acta. Haematol. 20: 246–252. 125 Haas, R. 1940. Über die Antigeneigenschaften von Papainpräparaten. Biochem. Z. 305: 280–289. 126 Habermann, E. & M. M. A. El Karemi. 1956. Antibody formation by protein components of bee venom. Nature. 178: 1349. 127 Halliday, R. & R. A. Kekwick. 1960. The selection of antibodies by the gut of the young rat. Proc. Roy. Soc. London Ser. B. 153: 279–286. 128 Hanan, R. & J. Oyama. 1954. Inhibition of antibody formation in mature rabbits by contact with the antigen at an early age. J. Immunol. 73: 49–53. 129 Harboe, M. 1959. A new hemagglutinating substance in the Gm system, anti-Gm. Nature. 183: 1468–1469. 130 Harboe, M. 1959. A new hemagglutinating substance in the Gm system, Anti-Gmb. Acta Pathol. Microbiol. Scand. 47: 191–198. 131 Harboe, M. & J. Lundevall. 1959. A new type in the Gm system. Acta Pathol. Microbiol. Scand. 45: 357–370. 132 Harris, H., S. D. Lawler, E. B. Robson & O. Smithies. 1960. The occurrence of two unusual serum protein phenotypes in a single pedigree. Ann. Human Genet. 24: 63–69. 133 Harris, H., D. G. Penington, E. B. Robson & C. R. Scriver. 1960. A further genetically determined transferrin variant in man. Ann. Human Genet. 24: 327–332. 134 Harris, H. & F. L. Warren. 1955. Occurrence of electrophoretically distinct haemoglobins in ruminants. Biochem. J. 60: 29. 135 Harris, H. & M. Whittaker. 1959. Differential response of human serum cholinesterase types to an inhibitor in potato. Nature. 183: 1808–1809. 136 Hartley, P. 1948. Behaviour of different types of homologous and heterologous diphtheria antitoxin when administered to pregnant guinea-pigs. Month. Bull. Min. Hlth. & Pub. Health Lab. Serv. 7: 45–54. 137 Hartley, P. 1931. The effect of peptic digestion on the properties of diphtheria toxin. Proc. Roy. Soc. London Ser. B. 138: 499–513. 138 Henderson, J. F. & G. A. LePage. 1959. The nutrition of tumors: a review. Cancer Research. 19: 887–902. 139 Henion, W. F., T. E. Mansour & E. Bueding. 1955. Immunological specificity of lactic dehydrogenase of Schistosoma mansoni. Exptl. Parasitol. 4: 40–44. 140 Henion, W. F. & E. W. Sutherland. 1957. Immunological differences of phosphorylases. J. Biol. Chem. 224: 477–488. 141 Henningson, K. & J. C. Nielsen. 1961. A rare phenotype within the Gm system. Nature. 192: 476–477. 142 Higashi, T., M. Yagi & H. Hirai. 1960. Immunochemical study on catalase. J. Biochem. Tokyo. 47: 696–698. 142a Hirs, C. H. W., S. Moore & W. H. Stein. 1953. A chromatographic investigation of pancreatic ribonuclease. J. Biol. Chem. 200: 493–506. 143 Hirschfeld, J. 1959. Immuno-electrophoretic demonstration of qualitative differences in human sera and the relation to the haptoglobins. Acta Pathol. Microbiol. Scand. 47: 160–168. 144 Hirschfeld, J. 1961. The use of immunoelectrophoresis in the analysis of normal sera and in studies of the inheritance of certain serum proteins. Sci. Tools. 8: 17–25. 145 Hirschfeld, J. 1962. The Gc-system. Immuno-electrophoretic studies of normal human sera with special reference to a new genetically determined serum system (Gc). Progr. Allergy. 6: 155–186. 146 Hirschfeld, J. & L. Beckmann. 1960. A new group-specific serum system (Gc-groups) in relation to blood and serum groups. Acta Genet. Statist. Med. 10: 48–53. 147 Hirschfeld, J., B. Jonsson & M. Rasmuson. 1960. Inheritance of a new group-specific system demonstrated in normal human sera by means of an immuno-electrophoretic technique. Nature. 185: 931–932. 148 Hoagland, M. B. 1955. An enzymic mechanism for amino acid activation in animal tissues. Biochim. Biophys. Acta. 16: 288–289. 149 Hoagland, M. B., P. C. Zamecnik & M. L. Stephenson. 1957. Intermediate reactions in protein biosynthesis. Biochim. Biophys. Acta. 24: 215–216. 150 Hoecker, C., S. Counce & P. Smith. 1954. The antigens determined by the H-2 locus: A Rhesus-like system in the mouse. Proc. Natl. Acad. Sci. U.S. 40: 1040–1051. 151 Holter, H. & H. Holtzer. 1959. Pinocytotic uptake of fluorescein-labelled proteins by various tissue cells. Exptl. Cell Research. 18: 421–423. 152 Housewright, R. D. & R. J. Henry. 1947. Studies on penicillinase; effect of antipenicillinase on penicillin-resistant organisms. J. Bacteriol. 53: 241–247. 153 Howes, D. W. 1959. The growth cycle of poliovirus in cultured cells. II. Maturation and release of virus in suspended cell populations. Virology. 9: 96–109. 154 Huisman, T. H. J., G. Van Vliet & T. Sebens. 1958. Some genetic and physiological aspects of two different adult haemoglobins in sheep. Nature. 182: 171–174. 155 Ingram, V. M. 1957. Gene mutations in human haemoglobin: the chemical difference between normal and sickle cell haemoglobin. Nature. 180: 326–328. 156 Ishizaka, K. & D. H. Campbell. 1959. Biologic activity of soluble antigen-antibody complexes. V. Change of optical rotation by the formation of skin reactive complexes. J. Immunol. 83: 318–326. 157 Itano, H. A. 1957. The human hemoglobins: their properties and genetic control. Advan. Protein Chem. 12: 215–268. 158 Jacob, F. & J. Monod. 1961. Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3: 318–356. 159 Jakobowicz, R., H. Crawford, J. J. Craydon & M. Pinder. 1959. Immunological tolerance within tlie ABO blood group system. Brit. J. Haematol. 5: 232–244. 160 Jerne, N. K. 1951. Study of avidity based on rabbit skin responses to diphtheria toxin-antitoxin mixtures. Acta Pathol. Microbiol. Scand. Suppl. 87: 3–183. 161 Jokay, I., G. Bot & T. Szilagyi. 1958. Die Antigeneigenschaften der Muskel-phosphorylase. Acta Physiol. Acad. Sci. Hung. 14: 155–161. 162 Kabat, E. A. 1954. Some configurational requirements and dimensions of the combining site on an antibody to a naturally occurring antigen. J. Am. Chem. Soc. 76: 3709–3713. 163 Kabat, E. A. 1956. Heterogeneity in extent of the combining regions of human antidextran. J. Immunol. 77: 377–385. 164 Kabat, E. A. 1957. Size and heterogeneity of the combining sites on an antibody molecule. J. Cellular Comp. Physiol. 50 ( Suppl. 1): 79–80. 165 Kabat, E. A. 1958. Immunochemical approaches to polysaccharide and mucopolysaecharide structure. In Ciba Foundation Symposium. Chemistry and Biology of Mucopolysaecharides. Pp. 42–58. J. & A. Churchill. London . 166 Kabat, E. A. 1960. The upper limit for the size of the human antidextran combining site. J. Immunol. 84: 82–85. 167 Kabat, E. A. & A. E. Bezer. 1958. The effect of variation in molecular weight on the antigenicity of dextran in man. Arch. Biochem. Biophys. 78: 306–318. 168 Kabat, E. A. & M. M. Mayer. 1961. Inhibition reactions. In Experimental Immunochemistry. Pp. 241–267. 2nd Ed. C. C Thomas. Springfield , Ill .