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Peripheral blood lymphocytes from 15 patients with variable immunodeficiency and severe panhypogammaglobulinemia were evaluated for B and T cell surface markers. B cells were enumerated by immunofluorescent detection of both surface immunoglobulin (Ig) and the ability to bind aggregated Ig complexes. T cells were identified by their ability to form nonimmune rosettes with sheep red blood cells. Four distinct patterns were observed which were designated types I-IV. Type I: six patients had normal percentages (8.5-19.0%) of Ig-bearing B lymphocytes. Type II: four patients were observed to have B lymphocytes (4.5-15.0%) which lacked fluorescence-detectable surface Ig. Type III: the peripheral blood of these four patients contained a subpopulation (11.3-20.0%) of lymphocytes which apparently lacked both B and T cell markers ("null" cells). Type IV: one patient's blood was characterized by a subpopulation (18.0-22.0%) of lymphocytes which bore both B and T cell markers. Patients of each type had some clinical features in common. It is concluded that evaluation of lymphocyte surface markers provides a means of separating patients with variable immunodeficiency and panhypogammaglobulinemia into distinct groups which appear to differ in the nature of their fundamental defect.

A nonimmunoglobulin protein with the molecular weight of 9,145 (protein AS) has been shown to be a principal component of the amyloid fibrils in different clinical types of amyloidosis. A protein component, antigenically closely related to protein AS, was detected in human sera. The protein AS-related component (protein ASC) was found in the sera of many groups of patients, including 48 out of 55 patients with various clinical types of amyloidosis. No structural relationship of protein ASC to the plasma component of amyloid was found. Protein ASC was also present with high frequency in the serum of diseases known to be frequently complicated by amyloidosis. In some cases, ASC was found in the sera of patients 2-3 yr before the diagnosis of amyloidosis was established. Protein ASC was also frequently found in hypogammaglobulinemia. Among normal individuals, protein ASC was seldom detected in the serum by our techniques, but there was a noticeable increase with age and during pregnancy. Moreover, a more sensitive technique, immunoelectro-osmophoresis, revealed protein ASC in a higher number of sera from both patients and normal controls. Thus protein ASC was suggested to be a normal serum constituent, usually present only in minor quantities. Under certain conditions, protein ASC increases considerably in serum, and may in such instances act as a precursor for the deposition of amyloid fibrils in the tissues.

Leukocytes from nine patients with acquired agammaglobulinemia were studied in vitro. Synthesis of deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) induced by phytohemagglutinin was measured by determination of the degree of incorporation of labeled precursor. Synthesis of both DNA and RNA was decreased in the agammaglobulinemic cells. The presence of an inhibitor in the patients' sera could not be demonstrated. These results suggest that the basic defect in agammaglobulinemia is cellular rather than humoral.