Abstract
Summary The antigenic characteristics of γA-globulin, γG-globulin, albumin and siderophilin from nasal secretions and sera have been compared and their sedimentation behavior studied by sucrose density gradient ultracentrifugation followed by specific quantitative assay of the concentration of these proteins in the gradient fractions. γG-globulin in whole nasal secretions had a mean sedimentation coefficient of 6.5 S ± 0.7 S (1 S.D.), closely similar to the sedimentation behavior of γG-globulin isolated from whole serum by DEAE-cellulose chromatography or by starch block electrophoresis. In contrast, γG-globulin in samples of whole serum showed a mean sedimentation coefficient of 7.3 S ± 0.6 S (1 S.D.). The population of γG-globulins present in nasal washings included the γGa (γ2a), γGb (γ2b) and γGc (γ2c) subclasses but was antigenically deficient with respect to γGd (γ2d) or possibly unidentified subclasses of γG-globulin present in serum. γA-globulin in both nasal secretion and serum showed considerable size heterogeneity. The major part of the nasal secretion γA-globulins sedimented between 9–14 S, while most of the serum γA-globulin was found in the 7–9 S region. γA-globulin, isolated by DEAE-cellulose chromatography from nasal washings, exhibited sedimentation behavior closely similar to that of the γA-globulin in whole nasal secretion. Nasal secretion γA-globulin, heavier than 9 S, possessed antigenic determinants not found in γA-globulin from serum, while 5–7 S γA-globulin from nasal secretion and γA-globulin from serum were antigenically similar. Samples of isolated nasal secretion γA-globulin from four out of five volunteers, however, lacked Inv allotypes, although all samples possessed antigens associated with both K and λ type light chains. Albumin and siderophilin in nasal secretions and serum had similar sedimentation properties, and the albumin in nasal secretions was antigenically identical with its serum counterpart. Comparison of the properties of tears and parotid saliva to nasal secretions from the same individuals revealed that γA-globulin in the three secretions had the same sedimentation behavior and antigenic characteristics.
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