By Roberto J. Poljak (auth.), R. A. Reisfeld, W. J. Mandy (eds.)
This sequence was once initially entitled modern themes in Immunochemistry, and quantity 1 bearing that identify was once released. Upon its editorial evaluate and whereas charting the improvement of destiny volumes, the editors started to feel that the notice "Immunochemistry" used to be a bit of restrictive in accordance with its current interpretation. Accompanying the growth of information in immuno biology is a requirement for causes in molecular phrases. because the rationale of the sequence is to concentration cognizance on learn on the molecular point in any point of immunology, the editors and writer felt the time period "Immunochemistry" may be changed with "Molecular Immunology." therefore, the sequence now bears a revised appellation, modern themes in Molecular Immunology. The editors believe this extra correctly displays the meant breath of the sequence. An apology is obtainable to writers, librarians, and different catalogers for the inconvenience this modification will reason. F. P. Inman common Editor Athens, Georgia March,1973 vii Preface The earliest explorers into immunology have been straight away faced by means of myriad molecular riddles which turned more and more advanced as immunochemical tech niques resolved one query basically to elevate ratings of others. whilst our wisdom of mobile immunology was once becoming remarkably quick, in past times twenty years fascinating experiments delineated the molecular constitution of immuno globulins. those joint advances not just formed the Gestalt of present-day immunology, yet cleared the path for an incisive molecular method of the demanding situations of research.
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6, 7c, and 7d) will not necessarily display the subunit arrangement (it should also be considered that in Figs. 7a and 7b the model has been raised at its Vend for photographic reproduction). It seems most likely that the way in which IgG molecules are deposited on electron microscope grids (providing the "top" view of Figs. 7a and 7b) prevents the detection of subunits, whereas the X-Ray Crystallographic Studies of Immunoglobulins 21 "side" view (Figs. , 1971) makes the subunits more evident. The 6 A Fab New structure provides a three-dimensional model to explain some of the physicochemical properties of immunoglobulin molecules.
V. AFFINITY LABELING AND TOPOWGY OF THE ANTIBODY SITE In an extensive series of studies Singer and his colleagues analyzed many of the structural features of antibody sites by affinity labeling. With a variety of 38 Givol antibodies of different hapten specificities and with anti-DNP antibodies from several species, affinity labeling with diazonnium reagents labeled tyrosine residues on both Land H chains with a remarkable similarity in the distribution of label between the chains (H/L ratio oflabel was between 2 and 4).
Approximately 6000 native amplitudes were Figure 8. Schematic model of the structure of an IgG molecule incorporating the structural features determined for the Fab fragment and extrapolating these structural features to the Fc region. (Reproduced from Poljak et al. (1972) with the permission of Nature. ) X-Ray Crystallographic Studies of Immunoglobulins 23 measured using a computer-controlled diffractometer. Six heavy atom derivatives were included in the phase refinement process. 80. The definition of the molecular boundaries and of the subunits confirms the results obtained in the 6 A resolution analysis.