By Alfred Nisonoff
The Antibody Molecule studies the literature resulting in present wisdom of the constitution of immunoglobulins. The e-book starts off through outlining a few of the simple structural features of immunoglobulins with no bringing up the references on which the data is predicated. Separate chapters keep on with overlaying the chemical nature of the energetic web site of an antibody molecule and mechanisms of interplay with hapten; the overall structural positive factors and houses of a number of the sessions of human immunoglobulin; and amino acid sequences of human and mouse L chains and of human and rabbit H chains. next chapters care for the evolution of the immunoglobulin periods; distinct homes of mouse, guinea pig, rabbit, and horse immunoglobulins; idiotypic specificities of immunglobulins; and the genetic regulate of antibodies.
This ebook is intended for immunologists who've no longer in my opinion saw the advance of this intriguing interval within the background of immunology. it's going to additionally supply worthwhile supplemental studying for the intense pupil or investigator who needs to get to grips with the character of the antibody molecule, its genetic keep watch over, and mode of motion.
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Additional resources for The Antibody Molecule
The relationship of structure to the immunogenicity of various types of synthetic polypeptides will not be considered (see 20,21 for discussions of this question). Methods used for the preparation of synthetic polymers are described in the references cited below. A. Size and Specificity of Active Sites of Antibodies to Polyalanyl Peptides Studies of the specificity of antibodies directed to poly-D- or poly-L-alanyl groups were reported by Schechter et al (22,23). (See 32 2. ) Rabbit antibodies were elicited by immunization with a protein carrier, ribonuclease, to which polyalanyl side chains were attached by reaction of the protein with the N-carboxy anhydride of alanine.
These findings had their inception in the investigations of Jerne (70) and of Eisen and Siskind (12). Quantitative experiments require the measurement of binding affinities, which are determined by thermodynamic properties. Thermodynamic parameters (AG°, AH0, and Δ50) have also been investigated in efforts to analyze the mechanisms of antigen-antibody reactions. For example, a high affinity could be attributable to a large negative value for the standard enthalpy change, Δ// 0 , or heat of the reaction, or to a large increase in entropy (Δ50) resulting from the antigen-antibody reaction, or to both.
Specificity to Synthetic Polypeptides 31 active site of the myeloma protein corresponded approximately to that of the pentamer. These results were strikingly similar to those obtained with induced antibodies. The effective size of the active site of the myeloma protein with anti-levan activity appeared to be somewhat smaller. A trimer of the basic subunit of levan, fructose, showed maximum inhibitory capacity on a molar basis. The similarity in the type of specificity noted in myeloma proteins and in induced antibody provides one type of evidence for the concept that myeloma proteins have all the properties of induced antibodies.
The Antibody Molecule by Alfred Nisonoff