Ciba Foundation Symposium - Experimental Tuberculosis: by Ciba Foundation

By Ciba Foundation

Chapter 1 Chairman's starting comments (pages 1–4): Arnold R. Rich
Chapter 2 The Proteins of the Tubercle Bacillus (pages 5–13): M. Stacey
Chapter three Chemical constitution and organic job of Mycolic Acids (pages 14–40): J. Asselineau and E. Lederer
Chapter four Mycobactin: A development issue for Acid?Fast Bacilli (pages 41–54): F. L. Rose and G. A. Snow
Chapter five Polysaccharide parts of the Tubercle Bacillus (pages 55–68): M. Stacey
Chapter 6 Granuloma?Producing homes of artificial Fatty Acids (pages 69–86): J. Ungarm
Chapter 7 Early Tissue Reactions to Tubercle bacilli and Their items (pages 87–101): A. A. Miles
Chapter eight Succinic Dehydrogenase job in Tuberculous Animals (pages 102–114): S.P. Martin, S.N. Chaudhuri, C.D. Cooper and R. Green
Chapter nine Biochemical elements that may effect the destiny of Tubercle Bacilli in Tissues (pages 115–130): James G. Hirsch
Chapter 10 Bacterial elements involved within the Early part of an infection (pages 131–143): Hubert Bloch
Chapter eleven Serological job of varied Fractions of tradition Filtrates of the Tubercle Bacillus (pages 144–162): Stephen V. Boyden and Ernst Sorkin
Chapter 12 The Serology of Tubercle Polysaccharides (pages 163–173): C. N. Iland and D.B. Peacock
Chapter thirteen The Chemical Nature of the Lipoidal issue of the Tubercle Bacillus accountable for the Induction of Tuberculous hypersensitive reaction (pages 174–187): S. Raffei, J. Asselineaud. and E. Ledererd
Chapter 14 Tubercle Bacilli as Immunological Adjuvants (pages 188–197): R. L. Mayer
Chapter 15 Relation among development Inhibitory estate of Monocytes for Tubercle Bacilli and allergic reaction to Tuberculin: An in vitro learn (pages 198–210): Emanuesl Suter
Chapter sixteen Tuberculous allergy and Desensitization (pages 211–224): George Brownlede and D. G. Madigan
Chapter 17 Tubercle Bacilli in contaminated Tissues Grown on Tissue tradition (pages 225–236): E. M. Brieger
Chapter 18 The function of Bacterial Multiplication within the institution of Immunity to Tuberculosis (pages 237–245): Hubert Bloch
Chapter 19 at the Mode of motion of Cortisone at the Pathogenesis of Tuberculosis and its Implications for the character of Genetic Resistance to the ailment (pages 246–260): Max B. Lurie and Peter Zappasodi
Chapter 20 The Mechanism keen on bought Immunity to Tuberculosis (pages 261–282): Sidney Raffel
Chapter 21 Human Lung Tissue Reactions to the Tubercle Bacillus with regards to Chemotherapy (pages 283–298): Georges Canetti
Chapter 22 impression of definite Surface?Active brokers at the Host?Parasite courting in Experimental Tuberculosis (pages 299–310): P. D'Arcy Hart and R. J. W. Rees
Chapter 23 the connection among the expansion requisites and the Pathogenicity of Isoniazid?Resistant Mutants of Tubercle Bacilli: A examine of the function of Host body structure in Susceptibility to Infectious illness (pages 311–339): G. Middlebrook
Chapter 24 A Pathogenetic dating among Tuberculosis and Leprosy: the typical Denominators within the Tissue reaction to Mycobacteria (pages 340–343): Max B. Lurie
Chapter 25 The Leprosy Bacillus and the Host response to It (pages 344–354): J. Lowe
Chapter 26 The response of the Host Tissue with regards to Mycobacterium lepr? (pages 355–363): R. G. Cochrane
Chapter 27 Immunological and Physiological foundation of Immunization in Tuberculosis and Leprosy (pages 364–387): John H. Hanks

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ASSELINEAU, J. (1954). Bull. chim. R. Acad. , 239, 1561. , BLOCH,H. and LEDERER, E. (1954). Biochim. biophys. Acta, 15, 136. LEDERER,E. (1950). Biochim. biophys. Acta, 5, 197. , GANZ,E. and LEDERER,E. (1951). C. R. Acad. , 232, 2050. ASSELINEAU, J . and GENDRE,T. (1954). Bull. chim. , 1226. ASSELINEAU, J. and LEDERER,E. (1949a). Bull. Chim. , Paris, 31, 492. ASSELINEAU, J. and LEDERER,E. (1949b). C. R. Acad. , 228, 1892. ASSELINEAU, J. and LEDERER, E. (1950). C. R. Acad. , 230, 142. ASSELINEAU, J.

POLGAR, N. J. ckem. , 1008. POLGAR, N. J. chem. , 1011. POLONSKY, J. and LEDERER,E. Bull. chim. , 504. PUDLES,J. VEme Congrks Intern. , Rome. , p. 99. PUDLES,J. and LEDERER,E. Bull. Soe. Chim. , Paris, 36, 759. RAFFEL,S . Experientia, 6, 410. RAMSEY, C. C. and PATTERSON, W. I. (1948). J . Assoc. off. agric. Ckem. 31, 441. ROBERTS,E. G. and ANDERSON, R. J. J. biol. , 90, 33. SPIELMAN, M. A. J. biol. , 106, 87. STALLBERG-STENHAGEN, S. and STENHAGEN, E. (1947). Arlciv. Kimi. Min. , 24B, No. 9. STEENKEN, W.

SNOW of mycobactin that has been obtained. Although the extraction was efficient and yielded up to 0 . 5 g. complex/100 g. dried Myco. phlei, the product was always reddish brown. No way was found of removing the colour, and alternative means had therefore to be devised for material suitable for degradation studies. An essential step was found to be the formation of the copper complex, which was prepared either from the aluminium complex or from extracts derived from the moist cells by a more laborious process involving the use of large volumes of methanol.

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