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PubMed1979

Serum IgG, IgM and slow alpha-globulin levels in carrageenan-treated rats.

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.

Animals↗
PubMed1995

Synthetic serum substitute (SSS): a globulin-enriched protein supplement for human embryo culture.

OBJECTIVE: The purpose of the present study was to evaluate whether an IVF protein supplement prepared from human serum albumin (HSA) and human globulins would retain performance characteristics equivalent to those reported for the commercial plasma expanders, Plasmatein (Alpha Therapeutics, Los Angeles, California) and Plasmanate (Cutter Biological, Miles Inc., Elkhart, Indiana). METHODS: Pronuclear-stage human embryos were randomly divided and cultured in human tubal fluid medium (HTF) supplemented with either HSA (5 mg/mL) or Plasmatein (10%, v/v; 5 mg/ml) as a means of indirectly assessing the effect alpha- and beta-globulins have on embryonic development. Those results coupled with the known composition characteristics of Plasmatein were used as the starting basis to formulate test lots of synthetic serum substitute (SSS). RESULTS: Significantly (P < 0.05) more of the human embryos cultured in Plasmatein supplemented medium reached the four-cell or greater stage by 40 hr postinsemination than a comparable group cultured in HSA alone. Lot 1 of SSS, formulated with HSA (84% of total protein) and human globulins (16% of total protein) and an aqueous lipoprotein fraction derived from human plasma (Excyte IV; Miles Diagnostics, Kankakee, Illinois), produced accelerated early embryonic growth relative to control murine embryos grown in the presence of Plasmatein, however, the percentage of the embryos reaching the hatched blastocyst stage was decreased (45 vs 100%). Human embryos from seven patients, randomized to HTF medium supplemented with Plasmatein or lot 1 of SSS, showed equivalent growth at 36-40 hr postinsemination. A microprecipitate developed in media supplemented with lot 1 after several days of culture. The Excyte IV concentration was reduced and, ultimately, eliminated from the subsequent and final prototype lots of SSS. Murine embryos grown in the presence of lipoprotein free SSS showed significantly accelerated (P < 0.01) growth at 17 hr postthaw compared to Plasmatein and all embryos progressed to hatching by 41 hr. Human embryos, randomized to either Plasmatein or lot 3 of SSS, showed significantly accelerated growth (P < 0.01) when scored at 38 hr following insemination. CONCLUSION: Synthetic serum substitute provides a convient, standardized means of adding protein to media used in assisted reproductive technology (ART) procedures.

Animals↗
PubMed1985

Electron microscopy of seed-storage globulins.

The quaternary structures of a range of seed globulins, including examples of both the so-called 7 S and 11 S types, have been examined by electron microscopy. The legume 7 S proteins, phaseolin (bean), beta-conglycinin (soybean), and vicilin (pea), appear as flat discs of diameter ca. 8.5 nm and thickness ca. 3.5 nm formed by association of three subunit domains. Phaseolin converts to an 18 S tetramer at acid pH, and images recorded under these conditions suggest that four of the 7 S protomer discs associate to form the faces of a regular tetrahedron. The classical 11 S seed globulins, cucurbitin (pumpkin) and legumin (pea), are approximately spherical molecules of diameter ca. 8.8 nm composed of six subunits. In contrast, the hexameric 10 S storage protein from lupin seed, conglutin gamma, appears toroidal in shape with outer diameter ca. 10.3 nm and thickness ca. 2.2 nm. These results indicate that constraints imposed on seed proteins by their role in sustaining the germinating plant may have allowed a variety of different globulin structures to accumulate in the protein-storage bodies of seeds.

Antigens, Plant↗
PubMed1994

High continuing pregnancy rates after in vitro fertilization-embryo transfer using medium supplemented with a plasma protein fraction containing alpha- and beta-globulins.

OBJECTIVE: To evaluate both the laboratory and clinical outcomes after IVF-ET using culture media supplemented with a plasma protein fraction (PPF, Plasmatein; Alpha Therapeutics, Los Angeles, CA) containing albumin and significant amounts of alpha- and beta-globulins. DESIGN: One-year clinical trial of a PPF with high globulin content as a medium supplement during IVF, embryo growth, and ET. SETTING: Fertility Center of San Antonio, a private, office-based center for assisted reproduction. PATIENTS: Ninety-eight couples, with women ranging in age from 26 to 46 years, undergoing 103 ovum retrievals for IVF-ET as treatment for infertility because of tubal factor, endometriosis, anovulation, uterine or cervical factor, male factor, and unexplained causes. MAIN OUTCOME MEASURES: Fertilization rate, zygote cleavage rate, clinical pregnancy rate (PR), continuing PRs, and implantation rates. RESULTS: Supplementation with PPF in insemination, growth and transfer medium resulted in a clinical PR of 41.5% per transfer with continuing PRs of 35.2% per retrieval, 37.2% per patient, and 38.7% per transfer. CONCLUSIONS: A PPF containing significant amounts of alpha- and beta-globulins can serve as an effective protein supplement to IVF medium, with outcomes manifested as high continuing PRs. These data indicate a potential role for glycoprotein components of serum in supporting healthy embryo growth in vitro, although the mechanism may relate more to the general physicochemical properties of this fraction than to the actions of a specific component.

Adult↗
PubMed1954

The persistence of bovine gamma-globulin injected as an antigen into rabbits; a comparison with its previously studied persistence in mice.

A sensitive biological test has been used to detect the persistence of minute traces of a foreign protein, bovine gamma-globulin, in the blood and livers of rabbits intravenously injected with it, as an antigen. At various intervals after injecting these rabbits (donors) serum or liver tissue was transferred from them to the peritoneal cavities of normal or unilaterally adrenalectomized mice (recipients) with the aim of rendering the latter hypersensitive to the antigen that might be persisting in the transferred materials; a state of affairs detectable, 2 days later, by the appearance of signs of reversed passive anaphylaxis when the recipient mice were intravenously challenged with a strong anti-bovine gamma-globulin rabbit serum. The protein persisted in the blood of the donor rabbits, in readily demonstrable amounts for 1 month, and in the blood of one animal, in minute traces, or as long as 6 weeks. It was detectable in the livers for 8 weeks. The persistence of bovine gamma-globulin in rabbits, which form circulating antibodies to it well, is not as long as that in mice, which form antibodies to it poorly, since in previous work with the mouse the antigen was found (1) in the blood after 8 weeks and in the liver for 14 weeks. Nevertheless the antigen persists in the rabbit much longer than is generally supposed. Indeed it can be found in the liver all through the period in which circulating antibody is demonstrable in the blood. Explanations for the phenomenon have been suggested. Its significance in relation to the mechanisms of antibody formation is obvious.

Animals↗
PubMed1960

Anuphylactic reactions in the skin of the guinea pig with high and low molecular weight antibodies and gamma globulins.

High molecular weight (19S) gamma-globulin produces passive cutaneous anaphylaxis (PCA) reactions with its specific antiserum only when it is used as intravenous antigen. Reversed PCA reactions cannot be produced when the 19S protein is injected intradermally in contradistinction to the results with 7S gamma-globulin. Antibodies of the high molecular weight class, when injected intradermally, also failed to give PCA reactions following antigen injection. Heterophile antibodies from the sera of patients with infectious mononucleosis, demonstrated to be entirely of the 19S type, gave negative reactions, while 7S heterophile antibodies from guinea pig did give reactions following intravenous injection of sheep cells. Anti-B isoagglutinins of the 19S class failed to react, while those of the 7S class of similar titer gave clear reactions following the injection of B substance. Evidence was obtained that 19S antibodies were capable of inhibiting the PCA reactions obtained with the 7S type, indicating that interaction with antigen occurred. The failure to elicit PCA reactions appeared to be due to an inability to fix to guinea pig tissues in a manner similar to that known for 7S antibodies and gamma-globulin.

Animals↗
PubMed1964

RECONSTITUTION OF 7S MOLECULES FROM L AND H POLYPEPTIDE CHAINS OF ANTIBODIES AND GAMMA-GLOBULINS.

Admixture of separated L and H polypeptide chains of 7S gamma-globulins under appropriate conditions has been found to result in the reconstitution of 7S molecules. The chains were mixed in 0.5 N propionic acid and when dialyzed into neutral aqueous buffers interacted to form reconstituted material in greater than 30 per cent yield. This material had sedimentation coefficients of 6S to 7S, a weight average molecular weight of 160,000, and its antigenic structure and electrophoretic properties were the same as those of 7S gamma-globulin. By the use of I(131) and I(125) labels on the different types of chains, combined with ultracentrifugation of chain mixtures in sucrose density gradients, the 7S product was found to contain both isotopes in ratios consistent with the presence of two L and two H chains. After hydrolysis with papain, the reconstituted material yielded products resembling S and F fragments. All of the isotope corresponding to L chains was found in the counterpart of the S fragment; the isotope corresponding to the H chain fraction was present in both fragments. The activity reconstituted from chains of a purified guinea pig antibody to f1 phage was found to be associated mainly with the 7S material. Hybrid molecules containing rabbit L chains and human H chains and of human L chains and rabbit H chains were formed by the same techniques of reconstitution. It was found that the interchain disulfide bonds of native 7S gamma-globulins could be broken and reoxidized, as could those of reconstituted 7S material. Reduced L and H chains mixed in propionic acid, dialyzed against neutral buffers containing mercaptan, then against neutral buffers in the absence of mercaptan, formed stable 7S molecules of molecular weight 160,000, which were dissociable only after reduction.

Animals↗
PubMed1964

H CHAIN SUBGROUPS OF MYELOMA PROTEINS AND NORMAL 7S GAMMA-GLOBULIN.

Through the use of a variety of antisera to isolated myeloma proteins, four subgroups of 7S gamma-globulin type proteins were readily distinguished. The first, the Vi subgroup, consisted of ten of 64 myeloma proteins studied. The second, the We group, contained the majority of myeloma proteins. The third, the Ge subgroup, included three of 50 myeloma proteins. The fourth remains ill-defined and appears heterogeneous. Counterparts for both the Vi and the Ge subgroup, were found in the Fr II gamma-globulin and in the normal gamma-globulin of all of a large number of individual sera studied. The unique antigenic character of both groups was localized to the H chains, although different determinants were involved for different antisera. An essential role of intact disulfide bonds was apparent with certain rabbit antisera. In addition to the special antigenic characteristics, the Ge subgroup showed in each instance a fast mobility for the F fragments produced by papain which was not found for other myeloma proteins.

Antigen-Antibody Reactions↗
PubMed1964

A STUDY OF RABBIT GAMMA-GLOBULIN ALLOTYPY BY MEANS OF HETEROIMMUNIZATIONS.

Representatives of two species, the chicken and the goat, were immunized by injection with Freund's adjuvant, of specific precipitates prepared from the antisera of rabbits with various allotypic specificities. The precipitation reactions of the resulting antisera with normal rabbit sera were studied in liquid and in gellified media. In these reactions the isotypic specificity and often one or the other of the allotypic specificities of rabbit gamma-globulin were involved. It was always easier to obtain antibodies against the specificities controlled by the alleles of locus b (Ab4, Ab5, Ab6) than of locus a (Aa1, Aa2, Aa3). The precipitation reaction of antibodies against a specificity of the a series could always be inhibited by an excess (nearly always moderate) of a serum lacking this specificity. A similar inhibition of the antibodies against the specificities of the b series was often impossible, especially if the antiserum had been collected after a second injection of immunizing material. The reactions of 58 Ab4(+) sera with a goat anti-Ab4 serum and of 28 Ab5(+) sera with a chicken anti-AbS serum were studied in gel tubes (simple diffusion). The constant observation of two precipitation zones due respectively to two types of molecules, Ab4(+) and Ab4(-) (or Ab5(+) and Ab5(-)), indicated the existence of an appreciable number of Ab4(-) or Ab5(-) molecules, even in supposed homozygotes. In the latter rabbits Ab4(-) or Ab5(-) molecules are b(-) molecules; i.e., molecules lacking the specificities of the b series. Measurements of the distances between the two zones in the reaction of 72 sera revealed significant differences between sera of individuals of the same phenotype, as well as systematic differences not only between sera of homozygotes and of heterozygotes, but also between heterozygotes of different genotypes. These measurements were used to evaluate the ratio of concentrations of the two types of molecules detected by each of the two antisera. The occurrence of b(-) molecules in every one of the fairly large number of sera studied indicates a new aspect of the heterogeneity of gamma-globulin. Although detected by means of allotypy, this heterogeneity is not dependent upon factors which vary with individuals. These results are discussed in connection with what is known of the structure of gamma-globulin.

Animals↗
PubMed1954

Plasma and tissue proteins produced by non-hepatic rat organs as studied with lysine-epsilon-C14; gamma globulins the chief plasma protein fraction produced by non-hepatic tissues.

The non-hepatic tissues in a perfused "carcass" (caudal half of the rat) maintain some physiological functions for as long as 5 to 6 hours of perfusion, including good clearance of lysine-epsilon-C(14) and glucose from the perfusate, and synthesis of both tissue and plasma proteins. The perfused "carcass" tissues incorporate only small amounts of lysine-epsilon-C(14) into the plasma proteins to an extent not markedly affected by the presence of the gastrointestinal tract, pancreas, spleen, or kidneys. This activity is found only in the globulin fraction obtained by sodium sulfate fractionation. No significant activity was detected in the plasma fibrinogen or albumin fractions. C(14)-labeled plasma proteins obtained from the eviscerated surviving rat 6 hours after intravenous lysine-epsilon-C(14) have been separated by zone electrophoresis. The gamma globulins contain most of the C(14) activity, with small but measurable activity in the beta and alpha globulins, and no activity in the albumin fraction.

Animals↗
PubMed1963

Antigenic determinants in fragments of gamma globulin from rabbit serum.

Peptic digestion of fraction III from papain-digested rabbit serum gamma-globulin produces a variety of smaller fragments. Some are too large to pass through a dialysis bag, and these retain the capacity to precipitate with antiserum to rabbit gamma-globulin. Others pass through the bag and fail to precipitate with antibody, but they can inhibit the precipitation of antibody with fraction III. This indicates that antigenic determinants of the gamma-globulin molecule are carried in these fragments.

Animals↗
PubMed1963

GAMMA-GLOBULINS: QUANTITATIVE RELATIONSHIPS IN HUMAN SERUM AND NONVASCULAR FLUIDS.

Three types of gamma-globulins, gamma(2), gamma(IA), and yim, are present in certain body fluids and secretions in proportions significantly different from those of normal human serum. A lthough ylA-globulin is present in only small amounts in serum, it represents a major fraction of the gamma globulin of tears, bile, saliva, colostrum, and fluid of the small intestine.

Amniotic Fluid↗
PubMed1964

ANTIBODY TO HEREDITARY HUMAN GAMMA-GLOBULIN (GM) FACTOR RESULTING FROM MATERNAL-FETAL INCOMPATIBILITY.

Multiple samples of serum from a Gm(a-) female mated to a Gm(a+) male were obtained before, during, and after each of four normal uncomplicated pregnancies and tested for antibody to human gamma globulins of differing genetic types. An agglutinator for the Gm(a) factor first appeared in the mother's serum during the third trimester of the fourth pregnancy. The newborn (male) was genotypically Gm(a+), since his serum contained, in addition to maternal Gm(a-) gamma globulin, small amounts of Gm(a+) gamma globulin.

Antibodies↗
PubMed1964

STRUCTURAL DIFFERENCES BETWEEN 2 TYPES OF "HEAVY CHAIN" DISEASE PROTEINS AND MYELOMA GLOBULINS OF CORRESPONDING TYPES.

Structural differences between two antigenic types (designated C and Z) of gamma-globulins, both of low molecular weight, produced in " Heavy chain" disease are revealed by their relative susceptibilities to enzymatic degradation by papain and the nature of the cleavage products. Corresponding structural differences exist between the respective type C and type Z myeloma gamma(2)-globulins. These structural differences are tentatively assigned to the H-chains, and more specifically to the portion of the H-chain contained in the fast-moving (F) fragment of papain-treated gamma(2)-globulins.

Biochemical Phenomena↗
PubMed1964

DEPENDENCE OF A GM(B) ANTIGEN ON THE QUATERNARY STRUCTURE OF HUMAN GAMMA GLOBULIN.

The antigens associated with the Gm(b) factor of human 7S gamma-globulin differ in Caucasoids and Negroids. The studies reported here show that an antigen, Gm(b(w)), associated with the Gm(b) of whites but not with that of Negroes, is present on the S (slow) fragment of 7S gamma-globulin obtained by digestion with papain or pepsin. All other Gm antigens thus far studied have been found on the F (fast) fragment. The antigens Inv(a) and Inv(b) were detected on isolated L-chains, and Gm(a) and Gm(b) were detected on isolated H-chains, but Gm(b(w)) was detected on neither. Recombining the H- and L-chains restored activity for Gm(b(w)) comparable to that of intact gamma-globulin

Antigens↗
PubMed1964

SUBCLASSES OF HUMAN GAMMA-2-GLOBULIN BASED ON DIFFERENCES IN THE HEAVY POLYPEPTIDE CHAINS.

Three subclasses of human gamma(2)-globulin (IgG) molecules were detected in normal human serum with antiserums prepared in monkeys. These subclasses, designated gamma(2a)-, gamma(2b)-, and gamma(2c)-globulins, have antibody activity. The distinguishing antigenic characteristics of each subclass were associated with the heavy polypeptide chains and the F (fast) fragments resulting from treatment of gamma(2)-globulins with papain.

Antigens↗
PubMed1983

[Elevation of the serum concentration of alpha- and beta-globulins and of a particular carcinoembryonic antigen by ultrasound exposure of liver tissue and CEA-active carcinomas].

The concentration of alpha- and beta-globulins in the serum can be increased by exposure of the globulin-producing tissue of the liver to ultrasound. The ultrasound intensities producing this effect are harmless according to our present knowledge. Especially the concentration of the globulin carcinoembryonic antigen in the serum can be increased significantly by exposure of CEA-producing carcinomas to ultrasound. There is to investigate the possibility of the early detection of CEA-producing tumors using a provocation test by way of increasing still normal spontaneous CEA-concentrations in the serum by insonation of body regions in question to significant pathologic serum concentrations.

Alpha-Globulins↗
PubMed1962

The use of hyperimmune antivaccinia gamma-globulin for the prevention and treatment of smallpox.

Smallpox prophylaxis studies having shown that the classical Jennerian type of vaccination may in some instances prove inadequate to prevent the development of the disease or may be contra-indicated for certain persons, attempts were made to evolve a method which could supplement or replace such vaccination. Investigations reported in this paper have demonstrated that the administration of gamma-globulin obtained from the sera of various animals hyperimmunized with vaccinia virus gives highly effective results in the prevention of different forms of experimental vaccinial infection. Encouraging results were also obtained with this gamma-globulin given prophylactically to 13 persons who had been in close contact with smallpox patients during an outbreak of this disease in Moscow in 1960. The author suggests that hyperimmune antivaccinia gamma-globulin of animal origin may also prove effective in the treatment of postvaccinal complications.

Humans↗