For the purpose of studying immunogenetic factors related to disease susceptibility to systemic lupus erythematosus (SLE), HLA-A, B and DR typing was performed by the standard lymphocyte microcytotoxicity test using 247 typing antisera in 34 Japanese patients with SLE and 51 healthy individuals.
The results obtained were as follows:
1) SLE patients with proteinuria had the association with HLA-BW 35 (phenotype frequency 50.0%, Relative Risk=7.5, corrected P<0.10), compared with normal control (11.8%). SLE patients without proteinuria had the association with HLA-BW 55 (phenotype frequency 35.0%, RR=8.6, Pc<0.10), compared with normal control (5.9%).
2) Patients with SLE had the strong association with HLA-DRW 9 (phenotype frequency 52.9%, RR=4.6, Pc<0.025), compared with normal control (19.6%).
3) All of the peripheral blood lymphocytes obtained from 10 patients with SLE who had anti-RNP antibody reacted with MT 3, which was one of the B-cell alloantisera including three antibodies against HLA-DR 4, DR 7 and DRW 9.
4) The linkage disequilibrium between HLA-BW 61 and HLA-DRW 9 was seen in the patients with SLE.

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The in vivo localization of anti-platelet antibodies on the bone marrow megakaryocytes and its subclass were studied in SLE and ITP by means of the peroxidase labeled antibody method. The in vivo IgG production by bone marrow and splenic lymphocytes by platelets stimulations was also examined in ITP and SLE.
The in vivo localization of IgG on the bone marrow megakaryocytes was positive in 5 out of 6 patients with ITP. Its subclass was IgG₃. The in vivo localization of IgG was demonstrated only in one of 7 patients with SLE and its subclass was IgG₁. Bone marrow and splenic lymphocytes produced IgG in vivo by the stimulation of platelets.

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The present investigation was designed to evaluate the efficacy of S-sulfonated gamma-globulin (S-GG), of which interchain disulfide bonds were selectively cleaved to give S-sulfonate groups. When S-GG is intravenously administered, it gradually reconverts into the original gamma-globulin (GG) and decays with half-life of about 24 days, comparable to that of GG.
Children with whooping cough were divided into two groups, one consisted of 37 cases (male: female=15: 22) received the combined therapy with S-GG (100 to 120 mg/kg, intravenous administration with drip infusion.) and antibiotics, and the other consisted of 52 cases (male: female=25: 27) treated with antibiotics alone.
Bronchodilators and cough remedy were given orally to all patients. The improvement of cough and the decreasing rate of lymphocyte per day were compared between two groups, and following results were obtained.
1. The improvement of coughing in the combined therapy group of S-GG and antibiotics was superior significantly to that in antibiotics therapy group in total cases. The similar results were observed not only in patients with severe cough (frequent paroxysms with cyanosis and/or apnea), but also in patients with moderate (frequent paroxysms) to mild (not so frequent paroxysms) cough.
2. The decreasing rate of lymphocytes in combined therapy group was higher than that of antibiotics therapy group either in the cases with lymphocyte counts of more than 15, 000/mm³, or in that of less than 15, 000/mm³.
It was concluded that the combined therapy with S-GG and antibiotics to whooping cough was of value. The reducing effect to lymphocytosis by S-GG suggests to be the neutralizing activity to leukocytosis or lymphocytosis promoting factor produced by B. pertussis.

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We assesed, using the mouse system, whether the human gamma-globulin preparations could neutralize the leukocytosis or lymphocytosis promoting factor (LPF) and histamine sensitizing factor (HSF) of crude LPF preparation extracted from the supernatant of the liquid culture of B. pertussis. Intact gammaglobulin (GG), S-sulfonated gamma-globulin (S-GG), and pepsin-treated gamma-globulin (P-GG) were used as gammaglobulin preparations in this study.
1. All gamma-globulin preparations (GG, S-GG, and P-GG) could neutralize the LPF and HSF.
2. The neutralizing activity to LPF was found even when the S-GG was administered 4 and 8 hours after the injection of crude LPF preparation. But the activity was diminished when S-GG was given 24 hours later. The neutralizing activity to HSF was found at 4 hours injection, but reduced at 8 and 24 hours injection of S-GG after the administration of crude LPF preparation.
3. All gamma-globulin preparations produced precipitin bands in counter-immunoelectrophoresis with the crude LPF preparation.
These results suggested the presence of neutralizing antibodies in the gamma-globulin preparations to LPF and HSF.

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We have studied on IgG type monoclonal immunoglobulins with antistreptolysin-0 (ASO) activity to elucidate the cause of the discrepancy between the results by streptolysin-O (SLO) inhibition assay (Rantz-Randall) and by passive agglutination assay, and obtained following results.
(1) ASO titer in the M-component varied extremely with the change of reaction order in Rantz-Randall method. This finding indicates that the M-component dose not affect on the target red blood cells for SLO but react directly with SLO.
(2) ASO activity in the M-component was almost completely dropped by reduction and alkylation of the M-component to H and L chains, but the ASO activity was recovered approximately 50% by recombination of H and L chain.
(3) SLO was adsorbed specifically by the M-component conjugated Sepharose column. This M-component column study showed that the affinity of SLO to the M-component increased tenfold in reduced form compared with acidified form.
(4) The hemolytic activity of SLO was completely lost by incubation at 56°C for 30minutes.
(5) The hemolytic activity of cell bound SLO was inhibited almost same degree with free SLO by the M-component. This result suggests that the M-component is an antibody against the hemolytic active site or the antigenic determinant close to the hemolytic site of SLO.
Based on above findings, it is concluded that the ASO activity in M-component is true antibody activity against SLO and the discrepancy between SLO inhibition assay and passive agglutination assay may be caused by the partial differences of SLO antigenicity used in each assay system.

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