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The Separation and Characterization of Proteins Intrinsic to Nasal Secretion

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, and Laboratory of Immunology, Bethesda, Maryland 20014

Abstract

Antiserum prepared in rabbits against nasal washings of adult male volunteers has identified by immunoelectrophoresis six intrinsic components in nasal secretions in addition to the plasma proteins previously identified. Lysozyme activity was associated with one of these components, named on the basis of its electrophoretic characteristics, the N.W. ₂ component. Further characterization of nasal secretion lysozyme demonstrated that it is a basic protein of low molecular weight with sedimentation properties similar to those of crystalline egg white lysozyme.

A-Globulin was the most abundant protein in nasal secretions and two types of this immunoglobulin, differing in molecular size, antigenic characteristics and relative abundance were found. The A-globulin present in highest concentration had gel filtration properties indicating a molecular weight probably in excess of 200,000 and possessed antigenic determinants in addition to those found on A-globulin of serum origin. A smaller amount of the A-globulin present had antigenic characteristics and gel filtration properties closely similar to, if not identical with, those of serum 7S A-globulin.

Influenza virus neutralizing activity and hemagglutination inhibiting activity were found exclusively in nasal wash fractions which contained A-globulin as the only detectable protein. None of the other plasma or intrinsic components identified in nasal washings were associated with these anti-influenza activities.

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