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PubMed1962

Enzymatically produced subunits of proteins formed by plasma cells in mice. I. gamma-Globulin and gamma-myeloma proteins.

Gamma globulin and antibody obtained from inbred C(3)H mice are split by papain and cysteine into fragments roughly one-third the size of the original Molecule (S(20,w) = 3.5S). The papain digests were characterized by starch gel electrophoresis and immunological methods. The highly heterogeneous fragments could be divided into two groups with distinct antigenic determinants (S and F), which were separated by DEAE ion-exchange cellulose chromatography. Approximately two-thirds of the fragments had S antigenic groupings and one-third had F antigenic groupings. These data are consistent with the view that mouse gamma globulin is split by papain and cysteine into three major fragments, two of which are of the S type and one of the F type. Antibody activity of the original molecule was present in the S fragments. Although the S fragments did not precipitate the antigen (hemocyanin) they were shown to bind antigen specifically in the manner of univalent antibodies. The S fragments of normal gamma-globulin were very heterogeneous with a broad spectrum of electrophoretic mobilities. Comparison of S fragments from slow and fast migrating globulins showed that the mobilities of the original gamma-globulin samples were largely reflected in the mobilities of their S fragments. Additional observations indicated that the F fragments also may help to determine the electrophoretic mobility of intact gamma-globulin molecules. S fragments of differing electrophoretic mobility were shown to have the same antigenic determinants, indicating that the structural differences responsible for the electrophoretic mobility differences were not involved in the antigenic groupings identified with rabbit antisera. The F fragments of normal gamma-globulin migrated more rapidly than the S fragments, were less heterogeneous, and showed several bands on starch gel electrophoresis. The F fragments differed antigenically from the S fragments, and had no antibody activity. Two groups of F fragments (F and F') were detected with some antisera. The gamma-myeloma protein (5563) formed in a C(3)H plasma cell tumor and similarly fragmented by treatment with papain and cysteine, produced much more discrete S and F components than were found in the normal gamma-globulin digest. The electrophoretic properties of the myeloma protein fragments were within the range observed for normal gamma-globulin fragments. Although the gamma-myeloma protein shares antigenic determinants with normal gamma-globulins it lacks some of the antigenic groupings present in the gamma-globulin preparation. Both S and F fragments from the myeloma protein share antigenic determinants with the corresponding fragments from normal gamma-globulin. In addition, both S and F fragments of normal gamma-globulin possess antigenic groupings not present in fragments of the gamma-myeloma protein, accounting for the antigenic deficiency observed on comparison of the gamma-myeloma protein with normal gamma-globulins.

Animals↗
PubMed1977

Development of an intravenous gamma-globulin with Fc activities. II. Reconversion of S-sulfonated human gamma-globulin into the original gamma-globulin.

The reconversion of S-sulfonated antitetanus gamma-globulin (S-GG) into the original gamma-globulin was studied. S-sulfonate groups in S-GG could be converted into disulfide bonds in vitro. The conversion restored the greater part of both complement-fixing and skin-sensitizing activities. S-GG administered intravenously formed interchain disulfide bonds again in vivo, which was accompanied by restoration of the C-dependent passive hemolytic activity. Intravenous injection of S-GG did not cause a significant decrease in serum complement level.

Biotransformation↗
PubMed1976

[Prophylaxis and therapy with gamma globulin. General characterization and clinical use of gamma globulin preparations].

For accurate evaluation of the usefulness of gamma-globulin treatment, the clinical indications for passive immune prophylaxis and immunotherapy and the specific characteristics of commercially available gamma-globulin preparations have to be considered. Detailed investigations of currently used gamma-globulin preparations have shown that as yet no ideal product is available. Classical standard gamma-globulin and, in particular, enzymatically treated (Gamma-Venin, Veinoglobuline) or chemically modified preparations (Gamma-Globulin i.v. SRK, Intraglobin) for intravenous use have some deficiencies and involve potential risks for the patient. Nor is the infusion of "fresh frozen plasma" a safe and generally applicable alternative to the use of gamma-globulin concentrates. Thus from the outset the preconditions for effective treatment with gamma-globulin are not optimal. Standard and hyperimmune preparations, given once intramuscularly, are suitable for the prophylaxis of viral and bacteriotoxic diseases. In patients apt to react abnormally it is important to distinguish clearly between the few accepted indications and those that are more doubtful. Anti-D immunoglobulin is essential for the prevention of Rhesus sensitization after the delivery of a Rhesus-positive child. In general, gamma-globulin is recommended for substitution therapy and for the prophylaxis of recurrent acute bacterial infections in patients suffering from transient, congenital and acquired antibody-deficiency states. In such cases, high doses of an intravenously administrable preparation with a relatively long biologic half-life are recommended. The evidence for the effectiveness of gamma-globulin treatment of bacterial infections in patients without manifest disturbance of humoral immunity is equivocal. This is true, for example, of the oft-recommended combined use of antibiotics and high doses of intravenous gamma-globulin which is said to provide optimum antibacterial and antitoxic protection. There is even less chance of obtaining beneficial effects if gamma-globulin is given as an "ultimo ratio" in severe generalized bacterial infections resistant to antibiotic treatment. Localized and predominantly chronic infections are barely influenced by gamma-globulin. It is still too early to make a final assessment regarding the place and value of immunoglobulin concentrates for prophylactic and therapeutic purposes. This will only be possible if a preparation becomes available which contains all immunoglobulins in a biologically optimum state and concentration, is well tolerated and can be given in adequate doses both intramuscularly and intravenously.

Complement System Proteins↗
PubMedDate not supplied

Hepatitis B immune serum globulin and standard gamma globulin in prevention of hepatitis B infection among hospital staff: a preliminary report.

In May 1973 a controlled double-blind clinical trail with prophylactic injects of hepatitis B immune serum globulin (antibody titer by passive hemagglutination 1:355,000) and standard gamma globulin (1:100) was started in Sahlgren's Hospital, Göteborg, Sweden. The annual attack rate of clinical hepatitis B in the three departments studied had been 5 to 8 per cent during recent years. A total of 118 members of the hospital staff were prophylactically treated while 125 staff members were unwilling to participate and received no prophylactic treatment. During the first 20 months of study nine cases of clinical hepatitis B with jaundice occurred within the untreated group (7.2 per cent) while three cases (2.5 per cent) were observed in prophylactically treated individuals. After decoding it was found that 60 individuals had received specific hepatitis B immune serum globulin while 58 had received standard gamma globulin. Two of the three clinical cases of hepatitis B occurred within the standard gamma globulin group. Both groups included two individuals with transient antigenemia only and the standard gamma globulin group also included four individuals with antibody seroconversion.

Antibody Formation↗
PubMed1960

Gamma globulin and antibody formation in vitro. I. Gamma globulin formation in tissues from immature and normal adult rabbits.

Gamma globulin formation in vitro by various tissues was studied using the incorporation of C(14)-L-lysine into a protein precipitable by a specific anti rabbit gamma globulin serum prepared in a sheep. It was demonstrated that the rate of gamma globulin formation in similar numbers of spleen cells is much higher if taken from an immunized rabbit at the height of antibody formation than that in normal spleen cells. Besides spleen, other tissues shown to form gamma globulin in normal adult rabbits were: peripheral lymph nodes, bone marrow, lung, mesenteric lymph nodes, appendix, and thymus. In tissues from newborn rabbits gamma globulin formation could not be demonstrated. Rabbits 1 week old already showed a beginning of significant gamma globulin formation in appendix tissue, followed approximately 3 weeks later by gamma globulin synthesis in spleen and thymus. Histological observations on these tissues were described and correlated with findings on gamma globulin formation. In the discussion an attempt has been made to relate these observations on newborn and immature rabbits to those available in the literature on antibody formation in newborn animals.

Animals↗
PubMed1975

Lack of B lymphocyte depletion from murine spleen cell populations by a human gamma-globulin, anti-human gamma-globulin column system.

It has been reported previously that enriched populations of mouse thymus-dependent (T) lymphocytes could be prepared by the use of a column procedure that is believed to remove selectively cells with receptors for antigen-antibody complexes. In our hands, this procedure does not selectively remove B lymphocytes but rather masks the surface immunoglobulin. Analysis of the column-passed cells revealed an apparent decrease in the percentage of immunoglobulin-bearing cells but little decrease in either the percentage of complement receptor lymphocytes or the mitogenic response to lipopolysaccharide. Furthermore, rabbit immunoglobulin could be detected on the surface of 35 to 45% of the cells emerging from the columns prepared with rabbit anti-human gamma-globulin (HGG). After overnight incubation, 30 to 40% of the emerging cells reexpressed mouse immunoglobulin on their surfaces. Adsorption of the antisera used to make the columns with mouse gamma-globulin (MGG) diminished the depleting capacity of the columns. We conclude from these observations that antibodies in the anti-HGG sera, cross-reactive with mouse immunoglobulin, account for the spacious depletion of B lymphocytes observed when cells are passed over these antigen-antibody complex columns.

Animals↗
PubMed1960

Immunological studies of human gamma-globulin. Relation of the precipitin lines of whole gamma-globulin to those of the fragments produced by papain.

Two major antigenic fragments were obtained from various purified gamma-globulin preparations after papain treatment. One, the F component, had a mobility faster than the original gamma-globulin and the second, the S component, had a slower mobility. Similar F and S components were also obtained with certain homogeneous myeloma proteins which were closely related to gamma-globulin immunologically. Additional minor antigenic components were detected with certain antisera. The technique of immunoelectrophoresis was particularly useful for bringing out the different antigenic constituents obtained after papain treatment. The F and S components as well as a midfraction were isolated by chromatography on DEAE-cellulose. These were immunologically homogeneous and could be utilized to absorb F and S antibodies from various antisera. The relative amount of F and S antibodies varied in different antisera from individual rabbits immunized with whole gamma-globulin. Whole gamma-globulin was separated by zone electrophoresis into a fast migrating and a more slowly migrating fraction. Each of these gave rise to F and S components after splitting with papain. The F components of the two gamma-globulins were similar in mobility, while the S components showed marked mobility differences although antigenically they were very similar. The mobility differences of the parent gamma-globulin appeared to be primarily related to the differences in the S component. Certain antisera against pathological gamma-globulins were found to give double lines with a wide variety of gamma-globulin preparations in agar diffusion. These were shown to be related to the F and S antigenic determinants of gamma-glubulin. This relationship was evident by a number of procedures utilizing both Ouchterlony plate techniques and immunoelectrophoresis. The question of whether these findings indicate heterogeneity of gamma-globulin in relation to the F and S antigenic components, or whether different antigenic groups on one molecule can give rise to separate lines in certain instances, is discussed.

Antibodies↗
PubMed1967

Studies of human anti-gamma-globulin factors reacting with pepsin-digested gamma-globulins.

Many sera from normal individuals as well as patients with various disease states contain agglutinating antibodies which show specificity for antigenic determinants of gamma-globulin revealed by pepsin digestion at pH 4.1. Sera containing such agglutinating activity as well as sera negative for these agglutinators contain low molecular weight (3S-5S) components of slow gamma-mobility which inhibit these agglutination reactions. Low molecular weight inhibitors show both auto- and isospecificity, and are antigenically related to the 5S pepsin fragment of gamma-globulin. A common situation is thereby revealed in which human anti-gamma-globulin antibodies showing specificity for pepsin-digested gamma-globulins are present in serum along with low molecular weight gamma-globulin components capable of inhibition. Autoreactivity or autospecificity of such anti-gamma-globulin factors is a phenomenon shared by both normal human sera and sera from patients with various disease states.

Adult↗