By Leonie Varin
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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.
Les animaux en perles by Leonie Varin