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At least 19 recordsLinked to original sources
PubMed1981

Polyclonal gammopathy with beta-globulin-gamma-globulin bridging. Two unusual cases.

Polyclonal gammopathy with beta-globulin-gamma-globulin (beta-gamma) bridging has been classically, though not exclusively, described with cirrhosis. We studied two unusual cases that exhibited polyclonal gammopathy with beta-gamma bridging. In the first case, the coexistence of Kaposi's sarcoma appeared with angioimmunoblastic lymphadenopathy. In the second, liver disease developed as a complication of alpha 1-antitrypsin deficiency and retroperitoneal malignant fibrous histiocytoma involving the porta hepatis.

Aged↗
PubMed1978

[Modifications in alpha 2 globulins, gamma globulins and in rheumatoid factor during gold salt therapy in rheumatoid arthritis].

A total dose of g 1.071, given as hydrosoluble salts for a 12 month period, showed a significant decrease in serum gamma globulins along with clinical improvement in 17 patients affected with rheumatoid arthritis. A decrease in alpha 2 globulins and in rheumatoid factor titre was observed too, but it was not significant. The data suggest that in rheumatoid arthritis the gold therapy might also be effective on the immunological disease mechanism.

Adult↗
PubMed1995

Adsorption and covalent immobilization of human serum albumin (HSA) and gamma globulins (gamma G) onto poly(styrene/acrolein) latexes with pyrene, dansyl, and 2,4-dinitrophenyl labels.

The poly(styrene/acrolein) latexes (P(SA)1 and P(SA)2), differing in poly(acrolein) content, were synthesized by the emulsifier-less emulsion-precipitation polymerization of styrene and acrolein. The fraction of poly(acrolein) in the surface layer was 0.35 and 0.50, for the P(SA)1 and P(SA)2 latex, respectively. Latexes were labelled with 2,4-dinitrophenylhydrazine (DNPH), dansylhdrazine (DAH), and 1-aminopyrene (APY). Surface concentration of labels varied from 4.20.10(-7) mol m-2 (for APY label on P(SA)1 latex) to 1.54.10(-6) mol m-2 (for DNPH label on P(SA)2 latex) reflecting the fraction of polyacrolein in the surface layer and bulkiness of the label. The differences between adsorption and covalent immobilization of human serum albumin and gamma globulins onto the P(SA)2 latex and onto its derivatives labelled with the 2,4-dinitrophenyl (DNP), dansyl (DA), and pyrene (PY) groups were small. The observation conforms to the hypothesis that polyacrolein forms domains on the surface of the P(SA) latexes and that after labelling some aldehyde groups are still available for the covalent immobilization of proteins. Labelled and parent latexes were used in the model slide and turbidimetric aggregation tests for the goat anti-HSA. The fluorescent latexes, labelled with APY and DAH, and latexes labelled and with DNPH were found to be suitable for the model tests, similarly as the nonlabelled ones, however, some differences in the sensitivity, depending on the presence and the nature of labels, were noticed. The standard goat anti-HSA serum (Sigma) was detected at maximum dilution equal to 2000 in the slide test, and in the dilution region from 1.8.10(3) to 4.7.10(6) times in the turbidimetric test.

Acrolein↗
PubMed1985

Hepatic transport and binding of rose bengal in the presence of albumin and gamma globulin.

Gamma globulin and albumin are compared with respect to their effects on the hepatic transport of rose bengal and with respect to the rates and affinities with which they bind this dye. The apparent intrinsic clearance of rose bengal is greater in the presence of albumin than in the presence of gamma globulin, and this difference increases with the protein concentration. Because the binding affinities of these proteins also differ, however, it cannot be concluded decisively that the mechanisms of dye removal are distinct. For both proteins the binding reaction rates as measured by stopped-flow spectrophotometry are much faster than the rate of convection along the sinusoid or the rate of removal of free dye by liver cells. The transport data and the binding rate constants are the basis for an extended theoretical model developed and analyzed in an accompanying report.

Animals↗
PubMed1981

[Clinical study on ceftezole in oral surgery. Clinical effect of ceftezole used jointly with gamma-globulin (Gamma-Venin) (author's transl)].

Ceftezole, an antibiotic of cephalosporin C derivative was applied to treatment in 39 patients with odontogenic inflammation or postoperative infections. The drug was administered intravenously (1-5 g/day) for the period of 5-10 days. Twenty of them were administered jointly with gamma-globulin (Gamma-Venin). Therefore, we compared clinically between the group of ceftezole with Gamma-Venin and the other group without it. But no difference was noticed statistically between these groups. No side effect was observed with throughout all the cases.

Adolescent↗
PubMed1964

EVIDENCE FOR SPECIES' DIFFERENCES IN THE EFFECT OF SERUM GAMMA-GLOBULIN CONCENTRATION ON GAMMA-GLOBULIN CATABOLISM.

The fractional rates of catabolism of isotopically labeled mouse, human, bovine, and guinea pig gamma-globulins and human serum albumin were determined in mice and in guinea pigs whose serum gamma-globulin and serum albumin levels were elevated by immunization or by injections of exogenous serum proteins. These serum proteins were also followed in mice with different serum gamma-globulin levels due to different bacterial environments. The fractional rates of catabolism of the labeled gamma-globulins from all species tested were markedly increased in mice with elevated gamma-globulins due to immunization; to injections of human, mouse, guinea pig, or rabbit gamma-globulins; to exposure to supra normal numbers of bacteria in the environment. Injections of bovine gamma-globulin were only partially effective, and injections of human serum albumin had no effect. The gamma-globulin catabolic rates were decreased in mice with subnormal serum gamma-globulin levels (germfree mice). The catabolic rate of human serum albumin was essentially the same in all mice in spite of differences in serum gamma-globulin levels. In contrast, elevation of the serum gamma-globulin levels by injections of exogenous gamma-globulins or by hyperimmunization with keyhole limpet hemocyanin produced no change in the fractional catabolic rates of the isotopically labeled gamma-globulins and labeled albumin in guinea pigs. Thus, a feedback mechanism for the control of the serum gamma-globulin concentration appears to be operative in the mouse, but not in the guinea pig. Guinea pigs immunized with antigens in complete Freund's adjuvant or a saline suspension of killed E. coli had an increase in the catabolic rates of all labeled proteins tested including human serum albumin. Evidence is presented that the mechanism of this increase in catabolism is not the same as that seen in mice with elevated serum gamma-globulin levels.

Animals↗