By G. E. W. (Editor) Wolstenholme
Chapter 1 Chairman's advent (pages 1–3): J. H. Humphrey
Chapter 2 Mechanism of Haemolysis through supplement (pages 4–57): Manfred M. Mayer
Chapter three Small Molecular Weight Inhibitors of supplement motion (pages 58–73): Elmer L. Becker
Chapter four Mechanisms of Activation of C?I and Inhibition of C?I Esterase (pages 74–98): Irwin H. Lepow, George B. Naff and Jack Pensky
Chapter five difficulties in opting for the websites of Synthesis of supplement elements (pages 99–119): G. J. Thorbecke, G. M. Hochwald, R. Van Furth, H. J. Moller?Eberhard and E. B. Jacobson
Chapter 6 Mechanism of the Damage?Producing Steps of Immune Haemolysis (pages 120–132): Michael M. Frank, Herbert J. Rapp and Tibor Borsos
Chapter 7 results of supplement on Sensitized Nucleated Cells (pages 133–154): Henry J. Winn
Chapter eight Immune Bactericidal and Bacteriolytic Reactions (pages 155–174): Louis H. Muschel
Chapter nine Electron Microscope stories of Immune mobile Lysis (pages 175–189): J. H. Humphrey and R. R. Dourmashkin
Chapter 10 supplement and the job of Phagocytes (pages 190–221): S. V. Boyden, R. J. North and S. M. Faulkner
Chapter eleven Immune Adherence (pages 222–241): D. S. Nelson
Chapter 12 supplement, Conglutinin and Immuno?Conglutinins (pages 242–280): P. J. Lachmann and R. R. A. Coombs
Chapter thirteen Differentiation in vitro of Antigen?Induced Histamine free up from Complement?Dependent Immune damage (pages 281–304): ok. Frank Austen and Kurt J. Bloch
Chapter 14 the potential function of supplement in Autoaggressive strategies (pages 305–322): H. J. Moller?Eberhard and A. P. Dalmasso
Chapter 15 The function of supplement in Haemolytic approaches in vivo (pages 323–342): P. L. Mollison
Chapter sixteen supplement and the Paroxysmal Nocturnal Haemoglobinuria crimson telephone (pages 343–373): Wendell F. Rosse and J. V. Dacie
Chapter 17 Chairman's final feedback (pages 374–376): J. H. Humphrey
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Extra resources for Ciba Foundation Symposium - Complement
This concept is completely open to further alterations as inore information comes in. Pondman: For study of the mechanism of complement fixation it is important to discover the order of fixation of the various subfactors, especially because of the differences in activities attached to them. I am led to believe that PIF is the factor which promotes the stability of the E A C ’ I , ~complex, ,~ or in other words, inhibits decay of this complex. It is essential then to know whether or not fixation of PlC globulin is a prerequisite for this inhibitory activity of PIF.
But this is too easy. From a biochemical standpoint, if the experiments are designed properly and if one allows for differences in rate constants and dissociability tendcncies, one should cxpect that the coinponcnts can be exchanged; and when it doesn’t work, one ought to search for the reasons rather than assume a priori that components cannot be interchanged. There are many instances where difficulty arises but I feel that much can be learned from their exploration. Becker:But surely, these rate constants and dissociabilities are precisely the point at issue; biochemically we know that homologous enzymes from different species can differ quite radically in their kinetic constants.
In agreement with these absorption experiments, we have found that aiiti-C’2 inhibits the reactivity of EACf1a,4,2a with the C’3 factors. However, ths type ofinhibition test is far less efficient than the direct neutralization of C’2, in the fluid phase; that is, only a portion ofthe inhibitory antibody is capable ofblocking cell-bound C‘2a. The agglutination of EAC’ 1a,4,2a by anti-C’2 also supports the view that C’2 is physically bound by EACf1a,4. Since it is difficult to prove rigorously that the agglutiiiogen is actually the C’2 molecule, the absorption of inhibiting antibody and the neutralization of cell-bound C’2 constitute more trustworthy evidence than that obtained by agglutination.