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PubMed1980

[A new immune serum globulin preparation for intravenous administration (author's transl)].

A new immune serum globulin preparation has been developed which is suitable for i.v. administration. This product was prepared from Cohn fraction II by selective reduction with dithiothreitol of one or more of the interchain disulfide bonds between the heavy chains and subsequent alkylation of the formed sulfhydryls (about 8--10 per 160 000 daltons) with iodoacetamide. The of these chemical reactions has been termed MISG (modified immune serum globulin). It is free of anticomplement activity, contains essentially all of the antibody potency of immune serum globulin, sediments as essentially a single entity with a sedimentation coefficient of about 7 S, has been freed of all reactants, is non-toxic, and in rabbits is antigenically with normal human immune serum globulin. MISG with its Fc fragment portion intact maintains its complement mediated function as evidenced by its opsonic activity against bacteria. MISG had been tested extensively in vitro, in animals, and in humans. Half-life measurements in humans averaged 22.4 days (range 15.5--28.7 days) and efficacy was demonstrated in a 2-year crossover clinical study in which MISG was compared with normal immune serum globulin administered i.m.

Chemical Phenomena↗
PubMed1997

Intravenous administration of human immune globulin in dogs with immune-mediated hemolytic anemia.

OBJECTIVE: To evaluate the efficacy and safety of intravenous administration of human immune globulin in the treatment of dogs with immune-mediated hemolytic anemia (IMHA). DESIGN: Prospective clinical trial. ANIMALS: 10 dogs with confirmed primary IMHA that had failed to respond to conventional immunosuppressive treatment (administration of prednisone and cyclophosphamide or azathioprine). PROCEDURE: Diagnosis of IMHA was confirmed by detecting spherocytosis or autoagglutination in blood smears and by excluding secondary causes of IMHA. Dogs were treated with human immune globulin (1 g/kg [0.45 g/lb] of body weight, i.v.) during a 6- to 12-hour period. Prednisone treatment was continued in all dogs, and cyclophosphamide treatment was continued in 4. RESULTS: Median duration of prior immunosuppressive treatment was 12.5 days. Short-term response could not be evaluated in 2 dogs, because they were given blood transfusions within 7 days after immune globulin treatment. However, there was a significant increase in mean Hct and hemoglobin concentration in 8 other dogs from day 0 to 28 after treatment. Five dogs had clinically meaningful responses to treatment. Three dogs were alive 12 months after treatment. There were not any adverse effects that could be definitively attributed to immune globulin treatment; however, thrombocytopenia was observed in 6 dogs after treatment, and evidence of thromboembolism was detected at necropsy in 5 of the 7 dogs that died. CLINICAL IMPLICATIONS: Human immune globulin may be useful for short-term stabilization of some dogs with IMHA; however, it did not appear to improve long-term survival.

Anemia, Hemolytic, Autoimmune↗
PubMed1998

Thermal stabilization of multimeric proteins: a case study with alpha-globulin.

Preferential interaction parameters of multisubunit protein, alpha-globulin and monomeric protein human serum albumin (HSA) were determined in different cosolvents using precision densitymetry. The apparent partial specific volumes were determined under both isomolal and isopotential conditions for alpha-globulin in 0.02 M glycine-NaOH buffer at pH 10 and the values were 0.692+/-0.002 and 0.688+/-0.001, ml/g, respectively, at 20.00+/-0.01 degrees C. From the partial specific volume data with cosolvents the preferential interaction parameter (xi3) and other thermodynamic parameters were calculated at different solvent concentrations. The (xi3) values increased with an increase in the solvent concentration up to 30% and reached a maximum with the values of-0.111+/-0.018 g/g and -0.076+/-0.012 g/g in sucrose and sorbitol, respectively. In glycerol the (xi3) values decreased with an increase in solvent concentration. The above data is further supported by thermal denaturation profiles in which the apparent thermal denaturation temperature (apparent Tm) of alpha-globulin shows an increase from 63 degrees C to higher temperatures in the order of sucrose, sorbitol and glycerol. Alpha-globulin showed coagulation due to protein interaction at temperatures above 50 degree C. The apparent Tm of 63 degrees C for control protein was increased significantly up to 75 degrees C in 40% sorbitol with two fold increase in the delta(S) values showing the increased structural stability of alpha-globulin. At high solvent concentration the protein gets dissociated and the resultant monomers are hydrated which was evident by fluorescence data and the difference spectral results with a 6nm red shift in the emission maximum and 2 nm blue shift in UV-absorption maximum arising out of perturbation of aromatic chromophores. The studies were performed both at native pH of 7.9 where the protein is in its oligomeric form and at pH of 10 where it is dissociated form and the results compared. The data showed that the solvent is excluded more from the protein vicinity in the dissociated state.

Densitometry↗
PubMed1982

The assessment of fetal-maternal hemorrhage by an enzyme-linked antiglobulin test for Rh immune globulin recipients.

An enzyme-linked antiglobulin test has been developed to detect and quantitate fetal-maternal hemorrhage. The test is applicable to postpartum screening of Rh immune globulin candidates. The enzyme-linked antiglobulin test has greater sensitivity than agglutination tests; it has fewer false positive results than acid-elution detection methods and offers advantages for use in routine clinical laboratories. Postpartum samples from 186 mother were assessed by the enzyme-linked antiglobulin test; only 20 samples (10.75%) has detectable fetal cells, and no patient had bleeding of more than the limit of 30 ml of whole blood for one vial of Rh immune globulin. No clinical or historic factors could predict the patient at high risk for fetal-maternal hemorrhage. The use of the enzyme-linked antiglobulin test also could permit the reduction of the postnatal Rh immune globulin dosage and salvage much of the Rh immune globulin now administered.

Alkaline Phosphatase↗
PubMed1958

G Gamma globulins in germ-free rats.

The electrophoretic fractions of serum proteins were studied up to the 5th generation in a colony of germ-free rats. The germ-free animals had significantly lower concentrations of beta and the gamma globulins, while the other fractions were within normal limits. Assuming that the gamma globulins survive equally long in the circulation in germ-free animals as in controls, the production of gamma globulins in normal rats is three times as rapid as in germ-free rats. This suggests that the normal flora of microorganisms is an important stimulant for the gamma globulin-producing cells.

Animals↗
PubMed1959

Gamma globulin production in germfree rats after bacterial contamination.

The earlier observed pronounced hypogammaglobulinemia in germfree rats of different ages has been confirmed. Using an immunologic technique the concentration of immunologic gamma globulins were found to vary between 10 and 15 per cent of the values observed in ordinary rats. Upon contamination of germfree rats with the normal microbial flora a pronounced lag phase was noted before the gamma globulin level became normal. This lag phase was most pronounced in growing rats. Newborn rats seem to start gamma globulin production more rapidly than older germfree rats. The response with regard to gamma globulin production on contamination of germfree rats with different types of bacterial cells through the natural routes is not identical.

Animals↗
PubMed1962

The antigenic structure of the polypeptide chains of human gamma-globulin.

The antigenic properties of the polypeptide chains of human 7S gamma-globulin have been related to two major non-cross-reacting antigenic determinants of the whole molecule. These determinants, called S and F, were obtained by hydrolysis of gamma-globulin with papain. Antisera against whole gamma-globulin and against S and F fragments were used in techniques of immune diffusion. Light (L) chains of gamma-globulin showed reactions of partial identity with S fragments, and thus are antigenically deficient with respect to these fragments. Antisera directed against F determinants did not react with L chains but did react with heavy (H) polypeptide chain preparations. In addition, the major component of H chain fractions did not appear to contain determinants in common with the S fragments. L chains of a gamma-myeloma protein were shown to be antigenically deficient with respect to the whole myeloma molecule, and antigenically identical with the Bence-Jones protein of the same patient. Correlation of these results with those of previous investigations have led to the conclusions that the S fragment which is known to contain the combining region of antibody molecules, consists in part of L chains or portions of L chains, and that the F fragment, which mediates several other functions of the whole molecule, is composed in part of portions of H chains.

Antibodies↗
PubMed1963

Sequences of synthesis of gamma-1 macroglobulin and gamma-2 globulin antibodies during primary and secondary responses to proteins, salmonella antigens, and phage.

The nature of the antibodies produced by the rabbit during the primary and secondary responses to T(2) phage, proteins, and the O and H antigens of Salmonella typhosa has been determined. Immune sera have been fractionated by zone electrophoresis, sucrose density ultracentrifugation, and anion exchange chromatography. The resulting fractions have been assayed by phage neutralization or hemagglutination (antisera to proteins) or bacterial agglutination. In confirmation and extension of earlier work from this laboratory, the primary response to these antigens, with the exception of the O antigen of the Salmonella, included the early synthesis of 19S, gamma-1 globulin antibody, and the later synthesis of 7S, gamma-2 globulin antibody. The primary response to the O antigen consisted of the synthesis of only a macroglobulin agglutinin. The secondary response to the proteins, including the H antigen of the Salmonella, comprised the early synthesis of large amounts of the 7S gamma-2 globulin antibody to the same level attained during the primary response. The secondary response to the phage consisted in the synthesis of 7S, gamma-2 globulin antibody alone. Treatment of the macroglobulin phage-neutralizing antibody with mercaptoethanol resulted in complete loss of its neutralizing activity. A working hypothesis to explain these observations was presented. A salient feature of this hypothesis was the suggestion that different cells synthesized the two distinct molecular forms of antibody. The significance of the sequential synthesis of the two forms of antibody is not known. It was proposed that the system for synthesis of macroglobulin antibody is an auxiliary system for antibody synthesis, perhaps the first to develop phylogenetically and ontogenetically. It is felt that the present observations indicate a clear-cut qualitative distinction between the primary and secondary responses to immunization whereby these responses might be identified in various experimental situations. It is also felt that these findings with the primary and secondary responses to various antigens in the rabbit may be of widespread occurrence in nature among a variety of species.

Animals↗
PubMed1965

ISOLATION OF BETA IF-GLOBULIN FROM HUMAN SERUM AND ITS CHARACTERIZATION AS THE FIFTH COMPONENT OF COMPLEMENT.

At least 3 complement factors were found necessary for the conversion of the thermolabile intermediate complex EAC'1a,4,2a to a thermostable state. One of these factors is the earlier described beta(1C)-globulin. The second, a heretofore unrecorded serum protein, beta(1F)-globulin. The third factor has not yet been defined as a discrete serum protein entity. Kinetic experiments indicated that beta(1C) reacted prior to beta(1F), which in turn seemed to precede the third factor in the reaction sequence. Therefore, the 3 components were tentatively designated the third (C'3), the fifth (C'5), and the sixth (C'6) components of complement, respectively. A procedure was developed allowing the isolation of highly purified beta(1C)-(C'3) and beta(1F)-globulin (C'5) and of partially purified C'6. With respect to its function in immune hemolysis, beta(1F)-globulin or C'5 was found to be closely dependent on the simultaneous presence of C'6. The hypothesis that C'5 and C'6 form a functional unit was supported by the finding that both components interact with each other in solution resulting in the formation of a complex. A similar complex was also found in fresh human serum.

Beta-Globulins↗
PubMed1964

CHANGES IN SERUM ALPHA-2 GLOBULINS IN RETICULOSES.

The total concentrations of alpha(2) globulin and two of its components, haptoglobin and caeruloplasmin, have been determined in the sera from 78 patients with primary malignant diseases of lympho-reticular tissue (reticuloses). The total alpha(2) globulin fraction was significantly raised only in Hodgkin's disease. The serum haptoglobin was also significantly increased in Hodgkin's disease and some other reticuloses, including acute leukaemia, lymphosarcoma, and reticulum cell sarcoma. The serum level of caeruloplasmin was raised in all reticuloses. There was possibly some correlation between the rise in haptoglobin and caeruloplasmin concentrations and the total alpha(2) globulin in Hodgkin's disease but this was not statistically significant. The significance of these results is discussed, and it is concluded that the increase in alpha(2) globulin which occurs in Hodgkin's disease is due to an increase in several of its components and not to a single component.

Alpha-Globulins↗
PubMed1976

Serum globulin changes in patients with craniocerebral trauma.

Investigations of serum total protein, albumin, alpha-1, alpha-2, alpha-2M, beta- and gamma-globulin changes are reported in 48 patients with craniocerebral trauma. Only alpha-2 and alpha-2M globulins showed important variations, the first rising to three to four times normal values (112% on average) and directly correlating with the amount of tissue lesions. Alpha-2M changes were rather irregular with a tendency to severe decrease during the first days in patients with a bad prognosis. Reasons for non-regular changes of alpha-2M are discussed. Alpha-1 globulin showed a similar though less marked increase. Gamma globulin, on average, was diminished in the first week.

Beta-Globulins↗
PubMed1996

Mothers at risk of alloimmunization to the Rh (D) antigen and availability of gamma-globulin at the Mexican Institute of Social Security.

Hemolytic disease of the newborn develops mainly when an Rh negative (D-) mother becomes sensitized and produces anti-Rh positive (anti-D) antibodies capable of hemolysing D+ fetal erythrocytes. Maternal alloimmunization can be prevented by the administration of anti-D gamma-globulin immediately after the birth of each Rh positive child. In order to identify the frequency of prevention of alloimmunization at the Instituto Mexicano del Seguro Social (IMSS), the amount of mothers at risk of sensitization from 1985 to 1995 was estimated from Rh and ABO blood group frequencies and with the number of deliveries and abortions at the Medical Institutions. Also, information in regard to the dose of gamma-globulin units purchased by the Institute of Social Security from 1985 to 1993 was obtained. The number of mothers at risk steadily increased from 16,616 in 1985 to 21,071 in 1995, amounting to a total of 203,203 in the 10-year period, while only 120,800 gamma-globulin units were purchased in that same period. The findings in this study suggest the need to define reasonable policies for the acquisition of gamma-globulin lots to prevent alloisoimmunization of mothers at risk.

ABO Blood-Group System↗
PubMed1964

LYMPHOID ORGANS AND NORMAL GAMMA-GLOBULIN IN THE RAT.

Serum gamma-globulin was determined in adult rats several months after total thymectomy, subtotal splenectomy, or a combination of total thymectomy, subtotal splenectomy, and subtotallymphadenectomy. The thymus apparently is of little importance in the production of normal gamma-globulin, but it may influence the production of albumin because a reduction of serum albumin was only seen in groups where thymectomy was performed. The spleen seems to produce normal gamma-globulin to a greater extent than lymphoid tissue elsewhere in the body.

Alpha-Globulins↗
PubMed1984

Rh immune globulin after genetic amniocentesis: impact on pregnancy outcome.

Although Rh immune globulin is commonly given to Rh-negative women undergoing genetic amniocentesis, there is little documentation of the necessity, efficacy, or safety of this policy. In this study, reproductive outcomes in 147 women each receiving 150 micrograms of Rh immune globulin after genetic amniocentesis were compared with those of an equal number of Rh-positive amniocentesis control women. No significant differences were found in the incidence of midtrimester pregnancy loss, mean gestational age at delivery, mean birth weight, or frequency of preterm deliveries (P greater than 0.05 for all parameters). While two antepartum stillbirths occurred in the study group and none in the control population, causes unrelated to Rh immune globulin administration were apparent for both fetal deaths (one multiple congenital anomaly syndrome, one abruptio placentae at 38 weeks). Of the 103 Rh-negative women giving birth to Rh-positive infants, none were overtly sensitized at the time of delivery. It is concluded that second trimester Rh immune globulin administration does not increase the risk of pregnancy loss.

Abortion, Spontaneous↗
PubMed1981

Isolation of the 12 S globulin from rapeseed (Brassica napus L.) and characterization as a "neutral" protein. On seed proteins. Part 13.

An isolation procedure for the 12 S rapeseed globulin is described which includes precipitation by dialysis, purification using gel chromatography on Sephadex G-200, and ion-exchange chromatography on DEAE-Sephadex A-50. The isolated globulin represents a neutral protein with an isoelectric point at pH 7.25--determined by isoelectric focusing--and a relation of the acidic to basic amino acid residues (epsilon Glu, Asp--Amide ammonia: epsilon Arg, Lys, His) of 1.0. As in other storage globulins high contents of glutamic (19%) and aspartic (10%) acid and a low content of sulphur containing amino acids are characteristic for the amino acid composition. Amongst the basic amino acids arginine has the highest percentage (7%). Opposite to results of other authors the sugar content of the globulin is low (0.5%). From the amino acid composition an average hydrophobicity according to Bigelow was calculated which amounts to be 1041 cal/res. (4.36 kJ/res.).

Amino Acids↗
PubMed1988

Binding of cellulose sulphates to the 12 S globulin and the low molecular mass basic protein fraction from rape seed in insoluble complexes.

The binding of two differently substituted cellulose sulphates (CS) with DS 0.50 and 0.33 to two main rapeseed proteins, the high molecular mass neutral 12 S globulin and the low molecular mass basic protein fraction ("albumin") in insoluble complexes at pH less than Pi (protein) has been studied using turbidimetric titration and chemical analysis of the supernatant after coprecipitation. The binding of both types of CS to the globulin at pH 3.0-2.5 at the precipitation occurs at a substoichiometric CS-protein mass ratio. This result has been obtained both by turbidimetric titration and chemical analysis. Contrary to that, the CS binding to the albumin is substoichiometric according to the turbidimetric titration and stoichiometric according to the chemical analysis. The CS-protein mass ratio in the coprecipitates obtained of pH 2.5 and 3.0 is nearly independent on the CS concentration applied for the precipitation of the albumin. There is a typical dependence on the CS concentration, however, for the globulin at pH 3.0, which becomes less pronounced at pH 2.5. The CS-globulin complexes form sharp turbidimetric titration curves at pH less than Pi (pH 2.5-5.5), the maximum position of which shifts to lower pH with increasing percentage of CS. The analogous titration curves for the CS-albumin complexes are broader, owing to the heterogeneity of the albumin fraction. Both polyanions exert a solubilizing effect at a molar excess on both proteins. Regarding the weight part necessary for precipitation (W insol.), forming stoichiometric complexes (W stoich.) and solubilization (W crit.) of the proteins, the following range can be written: W insol. less than W stoich. less than W crit.

Brassica↗
PubMed1996

Large scale procedure for fractionation of albumins and globulins from pea seeds.

The buffer extractable proteins of pea, albumins and globulins, were successively extracted in a large amount at a pilot scale. In order to preserve as much as possible the native structure of proteins, a selective solubilization step procedure was performed. Firstly, albumins were extracted with acetate buffer and secondly globulins with phosphate buffer of high ionic strength. Each extract was desalted by diafiltration without protein precipitation. From 15 kg of flour, 380 g of albumin fraction and 1000 g of globulin fraction were obtained with a protein content of 86.0% and 90.7% of dry matter respectively. The characterisation of albumin and globulin fractions by electrophoresis, ultracentrifugation and anion-exchange chromatography, showed that the cross-contamination of these two fractions was minimal.

Albumins↗
PubMed2000

Molecular evidence of complex tissue- and sex-specific mRNA expression of the rat alpha(2u)-globulin multigene family.

alpha(2u)-Globulin is well known to be a rat protein encoded by a highly homologous multigene family with more than twenty members. We report here the cloning and identification of major alpha(2u)-globulin mRNA species expressed in various tissues. Initially, eight individual clones (PGCL1-8) were obtained from a male preputial gland cDNA library. Data base analysis with BLAST demonstrated six mRNAs to be novel, all clones being characterized by highly conserved sequence motifs as lipocalins. All cDNAs contained an open reading frame of 543 nucleotides and encode 181 amino acid proteins showing 92.5-98.7% and 87.3-98.3% nucleic and amino acid identity, respectively. Denaturing gradient gel electrophoresis (DGGE) with sequence analysis showed that PGCL4 is a major member in the female mammary gland, and in the submaxillary and lachrymal glands of both sexes, while the counterpart in male liver and the coagulate glands was found to be PGCL1. Numbers of cDNA species including PGCL1 and PGCL4 were found in preputial glands, no sex-related difference being observed. These results directly demonstrate complex tissue- and sex-specific expression of alpha(2u)-globulins in terms of mRNA species, providing useful information for understanding regulation of the alpha(2u)-globulin multigene family.

Alpha-Globulins↗