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During the past few years there has been a rapid development in the chemical technology of epoxy resins. Currently, these resins are being widely manufactured and are available under a variety of trade names.Industrially the epoxy resins are important for use in corrosion-resistant surface coatings, molding compounds, castings, laminating or reinforcing plastics, encapsulating electronic circuits, and adhesives, as in metal-to-metal bonding.The generic name of these compounds is derived from the fact that they are polyethers with terminal epoxy groups. In general, they are condensation products of epichlorohydrin with p,p′-isopropylidenediphenol (bisphenol A) and have the type of chemical structure shown in the Figure (a). They have a wide range of viscosities, i. e., they range from low-viscosity liquids to high-melting-point solids. Commercial epoxy resins of the low-viscosity type usually contain, in addition to the high-molecular-weight resin, an epoxy resin modifier

Free-moving-boundary electrophoresis1,2 has facilitated the study of serum protein in both normal and disease states.3 In most disease states the electrophoretic pattern is nonspecific.4 However, characteristic changes do exist in hemophilia,5 lupus erythematosus,6 hypogammaglobulinemia, nephrosis, and multiple myeloma.3 In primary familial systemic amyloidosis free-moving-boundary electrophoresis has revealed the presence of a subclinical serum protein aberration.7It seemed possible that free-moving-boundary electrophoresis might detect a subclinical abnormality in the uninvolved members of a family in which clinical psoriasis was present. Since genetic factors are present in this disease,8,9 electrophoretic abnormalities were sought in such persons.MethodsA family, consisting of a mother, five children, and one grandchild, was selected for this study (Figure). A fasting blood specimen was drawn from each subject. Free-moving-boundary electrophoresis was carried out in barbital (Veronal) buffer, at pH 8.6 and ionic strength 0.1μ, according to

The antibiotic synnematin, isolated by Gottshall et al.,1 is produced by the mold Cephalosporium salmosynematum. It has been separated into components A and B by Olson, Jennings, and Junek.2 Synnematin B is active primarily against Gram-negative organisms, including Salmonella, some strains of Proteus, and strains of Shigella and Neisseria. Toxicity by intramuscular injection is reportedly negligible, both in animal experiments and in clinical studies of Salmonella infections.3,4 In a recent paper presented in the Proceedings of the Fourth Annual Symposium on Antibiotics a member of the Abbott Laboratories reported that synnematin B was seven times less toxic than penicillin in animals.5 The antibiotic has not been crystallized, and all material available for use was less than 50% pure.*In a personal communication to one of us (A. H. W.)5 it was called to our attention that two cases of pinta had been cleared