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PubMed1983

Post-gamma globulin. II. Radioimmunoassay determination of levels of post-gamma globulin and beta 2-microglobulin.

Post-gamma globulin previously isolated and partially sequenced in this laboratory was used for production of polyclonal and monoclonal (hybridoma) antibodies. A radioimmunoassay method was developed for quantitation of post-gamma globulin with either antibody. The titration curves obtained were treated statistically and found practically indistinguishable. The sensitivity of the method adopted for the quantitation of post-gamma globulin in a variety of biological fluids was 0.13 ng/ml and the upper limit of precision was 2.5 ng/ml. The following results were obtained (mean +/- 1 SD): normal sera, 0.96 +/- 0.20 microgram/ml; pregnancy sera, 1.08 +/- 0.28 micrograms/ml; cord blood 2.08 +/- 0.33 micrograms/ml; hospitalized patient's sera, 1.3 +/- 0.54 micrograms/ml; geriatric subjects' sera 2.26 +/- 1.10 micrograms/ml; cerebrospinal fluid, 5.37 +/- 3.36 micrograms/ml; saliva, 1.22 +/- 0.67 micrograms/ml; synovial fluid, 1.27 +/- 0.41 micrograms/ml and urine, 0.11 +/- 0.125 microgram/ml. To shed light on the catabolism of post-gamma globulin the levels of beta 2-microglobulin were also measured radiometrically. Correlative statistical analysis of all the data have shown that renal handling of post-gamma globulin and beta 2-microglobulin may be very similar but not necessarily identical.

Antibodies↗
PubMed1975

[Effect of gamma globulin on reactivity of the organism. V. Types of biological activity of gamma globulin preparations].

Biological activity of 110 series of commercial gamma-globulin preparations was studied; they were found to contain placental antigens, group-specific blood substances, gonadotropic hormones and antibodies to them. Placental antigens were found in 12% of placental and abortive gamma-globulin batches in titres of 1 : 2--1 : 16; no placental protein was revealed in donor gamma-globulin. There were group-specific blood substances in all the batches of placental and abortive gamma-globulin studied (in titres of 1 : 138--A, 1 : 112 B in the placental gamma-globulin and in titres of 1 : 48.9--A, 1 : 32--B in the abortive gamma-globulin). In the preparations from the venous blood group-specific substances were either absent or present in lowe titres only (1 : 2). The value of gonadotropic hormones in the placental gamma-globulin batches constituted 873+/-157, and in the abortive--991.4+/-147 IU/l; no gonadotropins were revealed in donor gamma-globulin. The mean titres of antibodies to gonadotropin hormone in the gamma-globulin preparations made of placental blood constituted 1 : 236+/-32, of abortive--1 : 131+/-16.6, and of the venous blood--1 : 46+/-24.7. The presence of biologically-active substances in the gamma-globulin preparations pointed to the necessity of increased requirement of their quality; additional requirements to its standardization proved to be also necessary.

Antibodies↗
PubMed1997

Induction of tolerance to human gamma-globulin in FcR gamma- and Fc gammaRII-deficient mice.

FcR gamma-deficient mice were used to examine the role of Fc gamma receptors in the induction of peripheral tolerance to human gamma-globulin (HGG). FcR gamma-deficient mice injected with HGG in adjuvant demonstrated a CD4+ T cell response to in vitro challenge with HGG, as assayed by proliferation, cytokine secretion, and Ag-specific help for B cell Ab production. In vitro kinetics of Ag-specific proliferation were similar in both conventional and knockout mice. Peripheral tolerance could be established in these mice with a single dose of deaggregated protein, despite the lack of functional Fc gammaRI, the high affinity receptor for monomeric IgG. Establishment of unresponsiveness was observed at both the T and B cell levels. T cell tolerance was manifested in the reduction of T cell helper function and Ag-induced release of Th1- and Th2-like cytokines, as well as decreased proliferation to Ag-specific stimulation. B cell tolerance was demonstrated in knockout and normal mice by failure to detect HGG-specific Ab production using an immunization protocol for Ab production that bypasses the need for Ag-specific T cells. These results demonstrate that induction of tolerance in CD4+ cells to HGG does not require transduction of a signal through Fc gammaRI. Furthermore, the ability to induce tolerance to HGG in B cells in Fc gammaRII-deficient mice suggests that down-regulation of Ag-specific B cells through Fc gammaRII is not the mechanism by which B cell tolerance is induced. However, Fc gammaRII plays a role in regulating the immune response since the Ab response to immunogenic HGG in Fc gammaRII-deficient mice is markedly enhanced.

Animals↗
PubMed1982

Post-gamma globulin : tissue distribution and physicochemical characteristics of dog post-gamma globulin.

An animal model (dog) was established to investigate physicochemical and biological parameters of a basic low molecular mass protein---post-gamma globulin (p-gamma). In this study the distribution of this 11 000 daltons (11 kdaltons) protein was determined in extracts of the number of tissues. Extracts of parotid gland, brain and kidney contained high amounts of "free" p-gamma globulin (11 kdaltons). Two higher molecular mass forms (34k and 27 kdaltons) of this protein were demonstrated in the kidney and brain extracts. Extracts of ovary and uterus were devoid of the 27 k moiety and kidney extracts lacked the "free" p-gamma globulin (11k). These studies indicate that p-gamma globulin may be a part of a much larger molecule or that p-gamma globulin may be associated with another yet unknown protein. These findings may be important for clinical and pathological studies in human kidney and central nervous system (CNS) diseases.

Animals↗
PubMed1976

Reconstruction of intact gamma-globulin from S-sulfonated gamma-globulin in vivo.

The conversion of the S-surfonate group in a peptide to a disulfide bond has been observed in vitro. This paper reports that the conversion of this group in human S-sulfonated gamma-globulin (S-GG) appeared to occur in vivo judging from the change in molecular weight of S-GG observed in the presence of sodium dodecyl sulfate (SDS) and the restoration of hemolytic activity.

Animals↗
PubMed1980

[Structure and biological properties of immunoglobulins and gamma-globulin preparations. II. Properties of gamma-globulin preparations].

Various gammaglobulin preparations have been analyzed with regard to content of IgG aggregates and percentage distribution of the four IgG subclasses. Their elimination from the plasma compartment was also studied in turnover experiments. Chief attention was focused on gamma-globulin preparations for intravenous use. The various preparations clearly differed in their subclass composition and metabolic behaviour. At present these results allow no conclusions concerning the efficacy of the various preparations in severe bacterial infections, since controlled clinical trials are still lacking. They should, however, be borne in mind when selecting a gammaglobulin preparation for a planned clinical trial.

Humans↗
PubMed1972

Anti-gamma globulins and chronic infection: comparative studies of the immune response to various bacteria and gamma globulin preparations.

A study of the relationship of clinical states associated with prolonged infection (bacterial endocarditis and osteomyelitis) and generation of serum anti-gamma globulins was made with particular reference to quantitative amounts of staphylococcal protein A in various infecting strains. No correlation between individual strain amounts of protein A and presence of anti-gamma globulins was detected. Thirty-eight rabbits were immunized intravenously with various strains of bacteria (Staphylococcus aureus, enterococci, Streptomyces viridans, pneumococci, pseudomonas, and Escherichia coli) for periods of 6 weeks, and antibacterial as well as anti-gamma globulin antibodies were assayed. No single group or strain of bacteria stood out as being more prone to produce anti-gamma globulins than others tested. Most rabbits developed anti-gamma globulins reacting with human gamma globulins, whereas the specificity for rabbit gamma globulin appeared more restricted. In 16 rabbits immunized with eight different strains of S. aureus, quantitative elevation of serum gamma globulin above 2.5 g per 100 ml often seemed to be correlated with presence of detectable serum anti-gamma globulins. By contrast 15 rabbits immunized with autologous or isologous rabbit gamma globulins in many instances developed extremely high titers of anti-gamma globulins showing primary specificity for human rather than rabbit gamma globulin. These studies further amplify the remarkably heterogeneous anti-gamma globulin reactivity associated with various types of immune response.

Animals↗
PubMedDate not supplied

[Spontaneous deamidation of gamma-globulin].

gamma-Globulin from human blood serum was incubated in thermostat at 37 degrees within 15, 30, 45, 60 and 72 days. Amount of readily and poorly hydrolyzed amide groups as well as an increase in amino acid content were estimated in the protein at zero time and at these periods. The sterility of the preparation was examined in each case. Spontaneous deamidation of gamma-globulin, observed during incubation, caused an increase in negative charge and altered electrophoretic mobility of the protein molecule. gamma-Globulin was attacked by prothelin more effectively as amount of amide groups was decreased in the protein. Spontaneous deamidation appears to be one of reasons of the protein molecules ageing.

Amides↗
PubMed1975

[Gamma globulin therapy of acute viral hepatitis. Studies on the therapeutic effect of gamma globulin on the course and late prognosis of manifested acute viral hepatitis in man].

In a prospective study 148 consecutive patients with biopsyproved acute viral hepatitis were observed serially and followed for 5 years. They were divided into three groups on the basis of being treated with high or low doses of gamma globulin and compared with a control group, not treated. As the efficacy of gamma globulin for the prophylaxis or modification of infectious hepatitis has been well documented by many investigators during the past 25 years, we were interested in evaluating the therapeutic effect of gamma globulin on the course of viral hepatitis. The purpose of the study was to determine the comparative efficacy of various doses of gamma globulin in preventing complications and in influencing the severity and the length of time of acute viral hepatitis and in preventing the development of chronic hepatitis and cirrhosis. For controlling the clinical, biochemical and histopathologic course 12 functional parameters were repeatedly measured under stable clinical conditions and 3--12 liver biopsies were performed in an individual patient using the Menghini needle with an intercostal approach. During the 5-year trial an overall of 825 liver biopsis were performed with this 148 patients. We conclude from this study, that in about 80% of patients with acute viral hepatitis recovery is complete, but takes several month's. A protracted course of 4 month's duration until recovery was found in 45 patients (30,4%), persistent hepatitis with recovery after 1--4 years duration occurred in 37 patients (25%), global liver necrosis with hepatic coma in 3 (2,3%), chronic hepatitis in 22 (14,8%), 8 of them as chronic aggressive hepatitis and cirrhosis in 3 (2,3%). The study demonstrated no therapeutic efficacy of gamma globulin in modifying the course or preventing complications of both AuAg+ and AuAg-neg. acute viral hepatitis in man. There was no striking difference in the groups treated with various doses of gamma globulin compared with a control group.

Acute Disease↗
PubMed1962

The nature of Bence-Jones proteins. Chemical similarities to polypetide chains of myeloma globulins and normal gamma-globulins.

The chemical relations among Bence-Jones proteins, myeloma proteins, and normal gamma-globulins have been investigated by a variety of means. Starch gel electrophoresis in 8 M urea of reduced alkylated Bence-Jones proteins yielded patterns of bands corresponding to those of the light (L) polypeptide chains of the dissociated myeloma protein from the same patient. One instance in which this correspondence was found was chosen for extensive study. Chromatography on carboxymethylcellulose in 6 M urea was employed to isolate the light (L) polypeptide chains and heavy (H) polypeptide chains of the completely reduced and alkylated myeloma protein. Isolation of similarly treated Bence-Jones protein from the same patient corroborated the correspondence to the L chains of the myeloma protein. Amino acid analyses indicated that the compositions of the Bence-Jones protein and the L chains of the myeloma protein were identical. Moreover, the thermosolubility properties and spectrofluorometric behavior of the isolated L chains and Bence-Jones protein were similar. Ultracentrifugal analyses of the L chains of normal human 7S gamma-globulin showed that their molecular weight in 6 M urea was 20,000. In aqueous solution their molecular weight was 41,000, suggesting that they exist as dimers under these conditions. The L chains of normal human gamma-globulin were found to have reversible thermosolubility properties similar to those of Bence-Jones proteins. The H chains of normal human gamma-globulin did not share these properties. Using spectrofluorometric methods, characteristic molecular transitions were found upon heating Bence-Jones proteins and L chains. These transitions were indicated by an increase in the intensity of fluorescence at well defined temperatures as well as by reversible shifts in the wavelength of maximal emission. The findings suggest that Bence-Jones proteins are composed of L chains of the type found in normal and pathological gamma-globu]ins.

Bence Jones Protein↗