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The Journal of Immunology, 1966, 97: 925-938.
Copyright © 1966 by The American Association of Immunologists, Inc.
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The Sedimentation and Antigenic Properties of Proteins in Nasal and Other External Secretions

Roger D. Rossen, William T. Butler, Wilton E. Vannier, R. Gordon Douglas, Jr. and Arthur G. Steinberg

From The United States Department of Health, Education, and Welfare, Public Health Service, National Institutes of Health, National Institute of Allergy and Infectious Diseases, Laboratory of Clinical Investigations, the Laboratory of Immunology, Bethesda, Maryland, and Western Reserve University, Department of Biology, Cleveland, Ohio

Abstract

The antigenic characteristics of {gamma}A-globulin, {gamma}G-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.

{gamma}G-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 {gamma}G-globulin isolated from whole serum by DEAE-cellulose chromatography or by starch block electrophoresis. In contrast, {gamma}G-globulin in samples of whole serum showed a mean sedimentation coefficient of 7.3 S ± 0.6 S (1 S.D.). The population of {gamma}G-globulins present in nasal washings included the {gamma}Ga ({gamma}2a), {gamma}Gb ({gamma}2b) and {gamma}Gc ({gamma}2c) subclasses but was antigenically deficient with respect to {gamma}Gd ({gamma}2d) or possibly unidentified subclasses of {gamma}G-globulin present in serum.

{gamma}A-globulin in both nasal secretion and serum showed considerable size heterogeneity. The major part of the nasal secretion {gamma}A-globulins sedimented between 9–14 S, while most of the serum {gamma}A-globulin was found in the 7–9 S region. {gamma}A-globulin, isolated by DEAE-cellulose chromatography from nasal washings, exhibited sedimentation behavior closely similar to that of the {gamma}A-globulin in whole nasal secretion. Nasal secretion {gamma}A-globulin, heavier than 9 S, possessed antigenic determinants not found in {gamma}A-globulin from serum, while 5–7 S {gamma}A-globulin from nasal secretion and {gamma}A-globulin from serum were antigenically similar. Samples of isolated nasal secretion {gamma}A-globulin from four out of five volunteers, however, lacked Inv allotypes, although all samples possessed antigens associated with both K and {lambda} 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 {gamma}A-globulin in the three secretions had the same sedimentation behavior and antigenic characteristics.






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