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Proceedings of the Royal Society of... Jan 1959
Topics: Biochemistry; Ceruloplasmin; Globulins; Oxidation-Reduction; Serum Globulins
PubMed: 13623853
DOI: No ID Found -
The Journal of Clinical Investigation Jun 1967Selected tissues from human embryos of 6 to 9 weeks' gestation, from rat fetuses of 15 days' gestation, and from rats 2 days of age were incubated with (14)C-labeled...
Selected tissues from human embryos of 6 to 9 weeks' gestation, from rat fetuses of 15 days' gestation, and from rats 2 days of age were incubated with (14)C-labeled amino acids. Immunoelectrophoresis of the culture fluid after incubation, using rabbit antisera against human and rat fetal serum proteins, followed by radioautography revealed that: 1) Radioactive alpha-fetoprotein was present in cultures of human liver, rat liver, and rat yolk sac, but not in cultures of human or rat brain, lung, heart, kidney, intestines, skeletal muscle, skin, or placenta; human yolk sac was not studied. 2) Radioactive transferrin was also present in rat yolk sac cultures, and the same protein was found in rat liver cultures as well. 3) Rat liver and rat placenta cultures both produced radioactive serum Ralpha(2)-globulin. Serum alpha-fetoprotein concentrations in the rat declined abruptly after birth to approximately half of the prenatal level by 2 to 3 days of age, in accord with the loss of the fetal membranes at delivery; the alpha-fetoprotein level then remained relatively constant until the rat was 6 to 8 days of age, after which synthesis of the protein was increasingly suppressed.
Topics: Animals; Bone and Bones; Brain; Carbon Isotopes; Culture Techniques; Extraembryonic Membranes; Female; Fetus; Heart; Humans; Immunoelectrophoresis; Intestines; Kidney; Liver; Lung; Muscles; Pregnancy; Pregnancy, Animal; Rats; Serum Globulins; Skin; Transferrin
PubMed: 6067376
DOI: 10.1172/JCI105590 -
The American Journal of Tropical... Nov 2016Passive immunization with anti-dengue virus (DENV) immune serum globulin (ISG) or monoclonal antibodies (Mabs) may serve to supplement or replace vaccination for...
Passive immunization with anti-dengue virus (DENV) immune serum globulin (ISG) or monoclonal antibodies (Mabs) may serve to supplement or replace vaccination for short-term dengue immune prophylaxis. In the present study, we sought to establish proof-of-concept by evaluating several DENV-neutralizing antibodies for their ability to protect rhesus macaques against viremia following live virus challenge, including human anti-dengue ISG, and a human Mab (Mab11/wt) and its genetically engineered variant (Mab11/mutFc) that is unable to bind to cells with Fc gamma receptors (FcγR) and potentiate antibody-dependent enhancement (ADE). In the first experiment, groups of animals received ISG or Mab11/wt at low doses (3-10 mg/kg) or a saline control followed by challenge with DENV-2 at day 10 or 30. After passive immunization, only low-titered circulating virus-neutralizing antibody titers were measured in both groups, which were undetectable by day 30. After challenge at day 10, a reduction in viremia duration compared with the control was seen only in the ISG group (75%). However, after a day 30 challenge, no reduction in viremia was observed in both immunized groups. In a second experiment to test the effect of higher antibody doses on short-term protection, groups received either ISG, Mab11/wt, Mab11/mutFc (each at 25 mg/kg) or saline followed by challenge with DENV-2 on day 10. Increased virus-neutralizing antibody titers were detected in all groups at day 5 postinjection, with geometric mean titers (GMTs) of 464 (ISG), 313 (Mab11/wt), and 309 (Mab11/mutFc). After challenge, there was complete protection against viremia in the group that received ISG, and a reduction in viremia duration of 89% and 83% in groups that received Mab11/wt and Mab11/mutFc, respectively. An in vitro ADE assay in Fcγ receptor-bearing K562 cells with sera collected immediately before challenge showed increased DENV-2 infection levels in the presence of both ISG and Mab11/wt, which peaked at a serum dilution of 1:90, but not in Mab11/mutFc containing sera. The results suggest that antibody prophylaxis for dengue might be beneficial in eliminating or reducing viral loads thereby minimizing disease progression. Our results also suggest that blocking FcγR interactions through Mab11 Fc engineering may further prevent ADE.
Topics: Animals; Antibodies, Monoclonal; Antibodies, Viral; Antibody-Dependent Enhancement; Dengue; Dengue Virus; Disease Models, Animal; Humans; Immunization, Passive; Immunoglobulin G; K562 Cells; Macaca mulatta; Receptors, IgG; Serum Globulins; Viral Load; Viremia
PubMed: 27645784
DOI: 10.4269/ajtmh.16-0319 -
British Medical Journal Apr 1953
Topics: Biomedical Research; Globulins; Poliomyelitis; Serum Globulins; gamma-Globulins
PubMed: 13032537
DOI: No ID Found -
British Journal of Experimental... Aug 1979Serum levels of IgM, IgG, slow alpha 1- and slow alpha 2-globulins were measured either by quantitative radial immunodiffusion (IgG) or immunoelectrophoresis (IgM and...
Serum levels of IgM, IgG, slow alpha 1- and slow alpha 2-globulins were measured either by quantitative radial immunodiffusion (IgG) or immunoelectrophoresis (IgM and slow alpha-globulins) during the 3-week period after i.p. injection of 50 mg potassium carrageenan. There was a significant elevation in levels of IgM and slow alpha 1-globulin, maximal on Day 4 and returning to normal by Day 14. Slow alpha 2-globulin was detectable within 24 h, reached a peak at Day 2, and was no longer measurable in most rats by Day 14. Levels of IgG however, were unaffected by carrageenan injection.
Topics: Animals; Carrageenan; Immunoglobulin G; Immunoglobulin M; Male; Rats; Stimulation, Chemical; Time Factors; alpha-Macroglobulins
PubMed: 92333
DOI: No ID Found -
Immunology Jul 1964Serum globulin levels and antibody against sheep red cells, (`O' and `H'), haemocyanin and pneumococcus type 3 capsular polysacharide (SSS III) were studied in C3H/Bi...
Serum globulin levels and antibody against sheep red cells, (`O' and `H'), haemocyanin and pneumococcus type 3 capsular polysacharide (SSS III) were studied in C3H/Bi and C57BL×C3H/Bi F hybrid mice thymectomized within 18 hours of birth. Thymectomized mice tend to recover more slowly than intact mice from the physiological hypo-γ-globulinaemia present 3–4 weeks after birth, but the majority of mice that survived beyond 6 weeks had serum globulin levels comparable to those in intact animals. Increased γ-globulin levels were observed in some thymectomized mice which survived for 7 weeks or more and the immuno-electrophoretic patterns sometimes resembled those seen in mice with γ myelomas. Macroglobulin (γ) was detected in the sera of thymectomized mice which contained normal amounts of γ-globulin. Total serum protein levels of groups of thymectomized and intact mice were not significantly different. The turnover rate of plasma albumin was also closely similar in both groups, but that of γ-globulin was accelerated in most of the thymectomized mice examined. Antibodies against SSS III, sheep red cell agglutinins and typhoid `H' agglutinins behaved as 7S globulins, in contrast with sheep red cell haemolysins which belonged to the 19S group. Antibody levels following primary stimulation with sheep red cells and antigens were usually, but not always, much lower in thymectomized mice than in intact control mice. However antibody levels against haemocyanin and SSS III were within the range of controls in more than half the thymectomized mice. Few thymectomized mice after stimulation with a mixture of three antigens failed to give a detectable antibody response to all the antigens, and some responded as well as did intact mice. The significance of these findings is discussed in relation to current theories of the function of the thymus in the development of immune responses. Many of the older thymectomized mice showed a characteristic wasting syndrome, but it is unlikely that a general failure of antibody response can account for this. Evidence for the presence of auto-antibodies against red cells or nuclear or cytoplasmic constituents was sought but was not found.
Topics: Agammaglobulinemia; Animals; Animals, Newborn; Antibody Formation; Autoantibodies; Immunization; Immunoelectrophoresis; Immunoglobulin G; Macroglobulins; Metabolism; Mice; Pigments, Biological; Polysaccharides; Polysaccharides, Bacterial; Research; Salmonella typhi; Serum Albumin; Spectrophotometry; Streptococcus pneumoniae; Thymectomy; Typhoid-Paratyphoid Vaccines; Ultracentrifugation; Vaccination; gamma-Globulins
PubMed: 14193155
DOI: No ID Found -
THE IMMUNOGLOBULINS OF MICE. V. THE METABOLIC (CATABOLIC) PROPERTIES OF FIVE IMMUNOGLOBULIN CLASSES.The Journal of Experimental Medicine Jul 1965The metabolic properties of immunoglobulin were investigated by comparing five classes of mouse immunoglobulin. Three forms of 7S immunoglobulin had different rates of...
The metabolic properties of immunoglobulin were investigated by comparing five classes of mouse immunoglobulin. Three forms of 7S immunoglobulin had different rates of catabolism. The fractional rates of catabolism were found to be about 13 per cent per day for 7S gamma(2a)-globulin; 25 per cent for 7S gamma(2b)-globulin; and 17 per cent for 7S gamma(1)-globulin. Catabolism of the three classes of 7S gamma-globulin (gamma(2a), gamma(2b), and gamma(1)) were prolonged at low serum 7S gamma-globulin levels and accelerated at high serum 7S gamma-globulin levels. Each of the 7S gamma-globulin components was influenced by the serum level of the other mouse 7S gamma-globulin components and by exogenously administered human 7S gamma-globulin. They were not appreciably altered, however, by the serum level of IgA (gamma(1)A-, beta(2)A-globulin). The progressively changing (longer) half-times observed in turnover studies of normal IgG (7S gamma-globulin) may be caused by catabolic heterogeneity of normal 7S immunoglobulins which are immunochemically and catabolically related to gamma(2a)-, gamma(2b)-, and 7S gamma(1)-myeloma proteins. These studies indicate that the 7S gamma(2a)-, 7S gamma(2b)-, and 7S gamma(1)-globulins share a common catabolic control mechanism. This mechanism is influenced by the serum level of each of these components, but is independent of the serum level of IgA (gamma(1)A-globulin) and probably is independent of IgM (gamma(1)M-globulin). Catabolism of IgA (gamma(1)A-, beta(2)A-globulin) and IgM (gamma(1)M-globulin) was much more rapid than the catabolism of the 7S gamma-globulins. The halftimes of the IgA and IgM were approximately 1.2 and 0.5 days respectively. The fractional rate of catabolism of IgA and IgM seemed to be independent of their serum concentration. The rate of catabolism, as well as the rate of synthesis, was shown to play a major role in determining the serum level of each class of immunoglobulin.
Topics: Animals; Germ-Free Life; Hemolysin Proteins; Humans; Immunochemistry; Immunoelectrophoresis; Immunoglobulin G; Immunoglobulin Isotypes; Macroglobulins; Mice; Proteins; Research; gamma-Globulins
PubMed: 14330751
DOI: 10.1084/jem.122.1.41 -
The Journal of Experimental Medicine May 1950X-radiation and nitrogen mustard administration inhibit the formation of precipitins for whole bovine serum and bovine serum gamma globulin in the rabbit. When specific...
Experimental hypersensitivity in the rabbit; effect of inhibition of antibody formation by X-radiation and nitrogen mustards on the histologic and serologic sequences, and on the behavior of serum complement, following single large injections of foreign Proteins.
X-radiation and nitrogen mustard administration inhibit the formation of precipitins for whole bovine serum and bovine serum gamma globulin in the rabbit. When specific antibody formation is inhibited by these agents, intravenous injection of a single large dose of bovine serum gamma globulin is not usually followed by the development of tissue lesions 9 to 11 days later, as occurs fairly regularly in control animals. A fall in titre of serum complement to very low levels for 3 to 5 days is closely correlated in time with the disappearance of antigen from the circulation following the intravenous injection of single large doses of bovine serum albumin and bovine serum gamma globulin. A rise in complement titre to normal levels occurs as antibodies appear in the serum. This sudden fall in complement titre is correlated with the development of characteristic lesions, and does not occur when antibody formation is inhibited. The data presented are interpreted as evidence in favor of the concept that the lesions are due to a reaction between antigen fixed in or on tissue cells and circulating antibody. The possible significance of serum complement in the pathogenesis of anaphylactic tissue lesions is discussed.
Topics: Anaphylaxis; Animals; Antibodies; Antibody Formation; Antigens; Cattle; Complement System Proteins; Hypersensitivity; Mechlorethamine; Rabbits; X-Rays; gamma-Globulins
PubMed: 15415506
DOI: 10.1084/jem.91.5.505 -
Acta Veterinaria Scandinavica May 1973The correlation between the formol-gel reaction and the concentration of different serum proteins was investigated in 289 cattle with chiefly chronic diseases. A close...
The correlation between the formol-gel reaction and the concentration of different serum proteins was investigated in 289 cattle with chiefly chronic diseases. A close correlation, though not linear, was found between the quantity of globulin and the time of gelification. A positive formol-gel reaction within 24 hrs. indicated an elevated globulin level in serum. Increasingly marked rises of globulin were observed with shorter gelification times. A negative formol-gel reaction after 24 hrs. showed that the globulin concentration was at normal level. The results are discussed in the light of the relevant literature. It is concluded that the formol-gel reaction is of diagnostic and prognostic value for clinical work within bovine medicine.
Topics: Animals; Blood Proteins; Cattle; Cattle Diseases; Formaldehyde; Methods; Prognosis; Serum Albumin, Bovine; Serum Globulins; Time Factors
PubMed: 4772604
DOI: 10.1186/BF03547400 -
American Journal of Kidney Diseases :... Dec 1997Human immunodeficiency virus nephropathy (HIVN) continues to challenge nephrologic consultative services at major urban institutions. Although noted in the literature,... (Comparative Study)
Comparative Study
Human immunodeficiency virus nephropathy (HIVN) continues to challenge nephrologic consultative services at major urban institutions. Although noted in the literature, the decreased incidence of peripheral edema in HIVN has been unexplained to date. In HIV patients, total proteins frequently are found to be elevated due to an elevated globulin fraction. The impact that plasma proteins, specifically globulins, have on the total oncotic pressure has not been reported in HIVN, but may play a role in the paucity of edema noted in this proteinuric population. To evaluate the contributions of serum globulin to the total oncotic pressure and the presence or absence of edema in HIVN, we randomly selected 27 patients with proteinuria greater than 2.5 g/24 hr and serum albumin less than 3.1 g/dL from patients presenting to the nephrology outpatient clinic at the University of Miami/Jackson Memorial Hospital. Seventeen of the patients (63%) had a known diagnosis of HIV infection (group 1). These patients were subdivided into two subgroups: those presenting with clinically evident edema on physical examination (n = 7 [41%]; group 1A) and those who had an absence of edema (n = 10 [59%]; group 1B). Conversely, group 2 comprised 10 patients without known HIV infection, of whom six (60%) had edema (group 2A) and four (40%) did not (group 2B). Blood pressures were noted, and mean arterial pressure was calculated using standard formulas. Serum albumin, serum total proteins, and urine total proteins were measured using standard laboratory methods. Oncotic pressures for albumin (alpha), globulin (beta), and total protein (c) were calculated using the following formula: COPpl = alpha(2.8c + 0.18c2 + 0.012c3) + beta(0.9c + 0.12c2 + 0.004c3). We used Student's t-test to analyze the data. There is no significant difference between the albumin concentrations of HIV patients without edema (group 1B) and non-HIV patients with edema (group 2A), with mean concentrations of 2.3 +/- 0.1 g/dL versus 2.3 +/- 0.15 g/dL, respectively (P = NS). Group 1B, however, has a total oncotic pressure of 17.1 +/- 1.5 mm Hg, whereas both groups with edema (groups 1A and 2A) have statistically significant lower total oncotic pressures (12.1 +/- 2.3 mm Hg and 12.9 +/- 1.1 mm Hg, respectively; P < 0.05). The globulin oncotic pressures may account for some of the differences in total oncotic pressures, being significantly higher for those patients without edema in group 1B compared with group 2A (7.1 +/- 0.9 mm Hg v 3.9 +/- 0.4 mm Hg, respectively; P < 0.05). In patients with HIV, however, the presence or absence of edema is mandated by albumin concentration because both groups have similar globulin concentrations (group 1A 3.1 +/- 0.1 g/dL v group 1B 3.8 +/- 0.3 g/dL; P = NS). Mean arterial pressure does not play a role in edema formation in this study because the HIV patients without edema had the higher blood pressures (group 1B 97.8 +/- 4.7 mm Hg v group 2A 84.7 +/- 5.5 mm Hg; P < 0.05). We conclude that globulins play an important role in maintaining oncotic pressure in low albumin states. HIVN patients with increased serum immune globulin may benefit from higher globulin oncotic pressure, delaying the onset of clinical edema in the setting of proteinuria.
Topics: AIDS-Associated Nephropathy; Adult; Aged; Blood Pressure; Blood Proteins; Blood Urea Nitrogen; Creatinine; Edema; HIV Enteropathy; HIV Seronegativity; Humans; Incidence; Middle Aged; Osmotic Pressure; Proteinuria; Serum Albumin; Serum Globulins
PubMed: 9398127
DOI: 10.1016/s0272-6386(97)90088-3