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In a patient with chronic lymphatic leukaemia severe autoimmunohaemolytic anaemia (NAIH) was observed with coexistence of cold incomplete IgM, warm incomplete IgG and warm haemolysins active against papainized erythrocytes in low pH medium. The serologic and immunochemical characteristics of autoantibodies are presented and the mechanism of their action in vitro is tentatively explained.

In a material of 768 sera obtained from blood donors and patients and 150 sera containing HBs antigen it was investigated whether the available animal sera (horse, swine, goat) with anti-HBs antibodies meet the requirements of diagnostic sera. It was found that none of these anti-HBs animal sera was better than the human serum used as yet. Only the specificity of horse anti-HBs antibodies was equal to the human serum, hence horse serum could be used for diagnostic purposes in routine investigations by the precipitation and complement fixation method. The swine and goat sera did not ensure detection of all HBs antigens which are detected using human or horse serum.

Complement-binding ability of three isolated monoclonal proteins of IgG class, their Fab, and Fc fragments was analyzed (including tests for the presence of polymers, aggregated forms and immune complexes), and the influence of two monoclonal IgG lambda proteins on fibrinogen conversion to fibrin was determined. Two proteins--IgG1 lambda and IgG3K--bound small amounts of complement only when tested in native form, but failed to bind complement after thermal aggregation. Papain-digestion of these proteins revealed a significant ability of complement binding by Fc fragments. The third protein--M-IgG1 lambda--bound large amounts of complement when used in its native form, but after thermal aggregation this ability decreased. This protein differs in structure from monoclonal Ig described here. It was shown by the atypical elution pattern of papain digest of M-IgG1 lambda from CM-cellulose and by the anticoagulative activity of this protein. In control tests with polyclonal immunoglobulin complement-binding ability increased after thermal aggregation of the immunoglobulin, Fc fragments of the polyclonal immunoglobulin bound lower amounts of complement than whole molecules. As already mentioned, the activity of the factor inhibiting fibrinogen-to-fibrin conversion was observed in only one of two tested proteins M-IgG lambda. This activity was not connected selectively with Fab fragment. In identical concentrations polyclonal IgG had no effect on fibrinogen-to-fibrin conversion.

Four proteins M class IgG were analysed in detail in view of their more rapid electrophoretic migration in starch gel among most proteins in this class. On the basis of these investigations two protein (from sera 212 and 244) corresponded to subclass IgG-4, one (serum 119) probably to IgG-4 with polyclonal impurities from other subclasses, and the fourth protein (from serum 210) to subclass 3 or 1. Since subclass IgG-4 contains the greatest amount of sialic acid residues of the remaining IgG subclasses finding of more rapid migration of the observed proteins seems to be due to this. A hypothesis has been put forward that if rapidly moving IgG do not belong to subclass 4 then they have, probably, atypically arranged carbohydrate groups, e.g. in Fab fragment. It was found also that the studied proteins M were carried during chromatography with DEAE cellulose only when a buffer with higher concentration of NaCl was used.

In 206 sera from the patients with different haematological disorders including 45 sera from patients with idiopathic thrombocytopenia, immune complexes were searched for, using the method of inhibition of latex-IgG agglutination by rheumatoid factor (RF) and C1q complement component. In the group of patients in 27 cases (13%) presence of endogenous RF was found. The sera of 149 patients (72.5%) inhibited RF and C1q. With the exception of sera from patients with thrombocytopenia, all the remaining ones either inhibited RF and C1q or contained endogenous RF. In the sera of patients with idiopathic thrombocytopenia the inhibitory factors were found in 46.5% and endogenous RF in 22.5%. In 12 patients in this group selected on clinical grounds the levels of immune complexes were investigated before and during 2 weeks after splenectomy. Apart from some changes immediately after this operation no significant differences were observed in the levels of immune complexes during this brief follow-up.

Seven preparation of Cl-estrase inhibitor (Clinh) were prepared from the serum form which factor IX had been absorbed previously. Despite always the same technique and conditions of isolation the degree of Clinh recovery differed, being sometimes fairly low, and ranging from 24% to 56% in relation to the initial plasma. The preparations contained cartain amounts of other proteins from the groups of alpha- and beta-globulins, particularly coeruloplasmin and components of complement C3, C4 and C9. The concentration of these components was low in relation to the concentration of the inhibitor. Some preparations contained also low amount of albumins. The preparation (about 20 thousand Clinh units) was transfused to a patient with congenital deficiency of Cl-esterase inhibitor at the time free of symptoms. The investigation of the blood obtained 30 minutes after transfusion showed complete inhibition of C-L-esterase. Administration of the preparation to the patient at the time of acute oedema caused in 5 episodes rapid regression of oedema or inhibition of its increase, in two cases no evident positive effect was obtained.