scholarly journals ANTIGENIC RELATIONSHIPS BETWEEN IMMUNE GLOBULINS AND CERTAIN RELATED PARAPROTEINS IN MAN

1961 ◽  
Vol 114 (4) ◽  
pp. 521-533 ◽  
Author(s):  
Edward C. Franklin ◽  
Denis R. Stanworth
Keyword(s):  
Biological Properties ◽  
The Other ◽  
Antigenic Specificity ◽  
Myeloma Proteins ◽  
Antigenic Properties ◽  
Immune Globulins ◽  
Γ Globulins ◽  
Antigenic Relationships ◽  
Gel Diffusion ◽  
Bence Jones Proteins

The antigenic properties of normal 19S γ-globulin, pathologic macroglobulins, ß2A-myeloma proteins, and Bence Jones proteins have been compared with 7S γ-globulin and the small 3.5S units derived from it by gel diffusion precipitin techniques. These studies demonstrate that the determinant groups on the 7S γ-globulin molecule responsible for the cross-reaction with each of the other proteins are associated with the two fragments of 7S γ-globulin which have the antibody-combining sites. The antigenic specificity of the 7S γ-globulin which distinguishes it from each of these proteins is associated primarily with the fragment that is richest in hexose and can not combine with antigen. However when compared with certain of the paraproteins additional antigenic specificity was also found to reside in the fragments with antibody-combining activity. The finding of similar antigenic relationships in rabbit γ-globulins suggests that some of the biological properties associated only with the 7S γ-globulins and not with the other immune globulins may reside in the fragment which also carries the antigenic specificity of the protein.

Occurrence of Myeloma-Like γ-Globulin in C.S.F of A Four-Month Old Infant with Hydrocephalus

PEDIATRICS ◽  
1964 ◽  
Vol 33 (3) ◽  
pp. 435-440
Author(s):  
G. M. HOCHWALD ◽  
G. J. THORBECKE
Keyword(s):  
Paper Electrophoresis ◽  
Reticulum Cell ◽  
Reticulum Cell Sarcoma ◽  
Myeloma Protein ◽  
Characteristic Appearance ◽  
Myeloma Proteins ◽  
Group I ◽  
Immune Globulins ◽  
Γ Globulins ◽  
Narrow Bands

Myeloma-like immune globulins present themselves as narrow bands upon paper electrophoresis, and usually show a characteristic appearance in immunoelectrophoresis. Two antigenically different groups of myeloma proteins have been described: groups I and II. Recently, 60% of normal γ-globulin, throughout the mobility range of γ-globulin, has been shown to possess the antigen characteristic for group I, and 30% that for group II myeloma. Occurrence of myeloma-like proteins in the serum is not restricted to multiple myeloma. They may also be seen with other tumors, such as reticulum cell sarcoma, and various carcinomas. In addition, Sonnet and Milhaux have reported on the frequent occurrence of myeloma-like ("monoclonal") γ-globulins in the serum of adult Bantus with different diseases. When large amounts of a myeloma protein are present in the serum, it may be found in a much lower concentration in the spinal fluid.

scholarly journals GENETIC CHARACTERS OF HUMAN γ-GLOBULINS IN MYELOMA PROTEINS

1962 ◽  
Vol 116 (5) ◽  
pp. 719-738 ◽  
Author(s):  
M. Harboe ◽  
C. K. Osterland ◽  
M. Mannik ◽  
H. G. Kunkel
Keyword(s):  
Plasma Cells ◽  
Protein Product ◽  
Myeloma Protein ◽  
Myeloma Proteins ◽  
Normal Individuals ◽  
Γ Globulins ◽  
Normal Human ◽  
Genetic Characters ◽  
Single Plasma ◽  
Bence Jones Proteins

The genetic factors Gm(a), Gm(b), Gm(x), and Inv(a), Inv(b) described for normal human γ-globulin were all found in different myeloma proteins. A single myeloma protein never contained more than one product of alternate alleles even in heterozygous individuals. However, factors determined by the two different loci were often found in the same myeloma protein. The Gm(a) character of the myeloma protein parallelled that of the normal γ-globulin of the same serum in most cases. In contrast, the Gm(b) character was usually absent in the myeloma protein when it was directly demonstrable in the normal γ-globulin. The myeloma proteins from six Negroes were Gm(a+b-), whereas the normal γ-globulin was Gm(a+b+). This indicates that the effect of gene Gmb is similar in Negroes and whites, even though its relation to gene Gma is different in the two races. Gm factors were found only in the 7S γ-globulin type myelomas and not in other products of plasma cell tumors. Inv characters were, however, present in all four types of proteins studied, namely 7S and 19S γ-globulins, ß2A-globulins, and Bence Jones proteins. In two instances, genetic heterogeneity of the protein products was demonstrated suggesting the proliferation of more than one clone of plasma cells in some multiple myeloma patients. The accumulated evidence obtained in this study strongly suggested that the presence and absence of genetic characters was compatible with the concept that myeloma proteins were closely analogous to individual moieties in the spectrum of normal γ-globulins rather than truly abnormal proteins. Their study offered evidence of a heterogeneity of genetic characters among the normal γ-globulins in a given individual. It also appears probable that in normal individuals single plasma cells have a restricted capacity to express genetic information in their protein product.

scholarly journals PROTEIN-PROTEIN INTERACTIONS AMONG L POLYPEPTIDE CHAINS OF BENCE-JONES PROTEINS AND HUMAN γ-GLOBULINS

1964 ◽  
Vol 119 (5) ◽  
pp. 817-836 ◽  
Author(s):  
J. A. Gally ◽  
G. M. Edelman
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Bence Jones Protein ◽  
Thermally Induced ◽  
Myeloma Proteins ◽  
Group I ◽  
Γ Globulins ◽  
Normal Human ◽  
Polypeptide Chains ◽  
Bence Jones Proteins

The L polypeptide chains of certain Bence-Jones proteins of group I have been found in three forms: monomers of molecular weight of about 20,000, dimers which monomerize in dissociating solvents, and dimers which are stable in such solvents. The L polypeptide chains of some Bence-Jones proteins of group II were found to occur naturally only as stable dimers. The L chains of normal human γ-globulin have been obtained in a reduced unalkylated form, and a fraction of these chains was found to form stable dimers under oxidizing conditions. It is suggested that a single disulfide bond is involved in stabilization of the dimer. In experiments on the reconstitution of 7S γ-globulin, it was found that stable dimers of L polypeptide chains did not associate appreciably with Hγ chains to form a soluble product. L chains in the monomeric form, both of a reduced alkylated Bence-Jones protein and of reduced unalkylated γ-globulin, combined with Hγ chains to form a 7S product. After hydrolysis with papain, the 7S material containing the Bence-Jones L chains yielded fragments comparable to the fragments of papain-treated myeloma proteins. As indicated by spectrofluorometric measurements, dissociable dimers and stable dimers of the L chains of a Bence-Jones protein both underwent identical thermally induced transitions in the temperature range 48–58°C. When L polypeptide chains were present in reduced alkylated γ-globulin or reduced alkylated S fragments, no transition occurred until 65°C, the coagulation temperature of γ-globulin and S fragments. Above this temperature, L chains were released into solution. These experiments suggested that free L chains and L chains bound to Hγ chains have different conformational stabilities.

scholarly journals THE IMMUNOGLOBULINS OF MICE

1965 ◽  
Vol 122 (1) ◽  
pp. 41-58 ◽  
Author(s):  
John L. Fahey ◽  
Stewart Sell
Keyword(s):  
Serum Level ◽  
Control Mechanism ◽  
High Serum ◽  
The Other ◽  
Fractional Rate ◽  
Myeloma Proteins ◽  
Mouse Immunoglobulin ◽  
Γ Globulins ◽  
Metabolic Properties ◽  
Low Serum

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 γ2a-globulin; 25 per cent for 7S γ2b-globulin; and 17 per cent for 7S γ1-globulin. Catabolism of the three classes of 7S γ-globulin (γ2a, γ2b, and γ1) were prolonged at low serum 7S γ-globulin levels and accelerated at high serum 7S γ-globulin levels. Each of the 7S γ-globulin components was influenced by the serum level of the other mouse 7S γ-globulin components and by exogenously administered human 7S γ-globulin. They were not appreciably altered, however, by the serum level of IgA (γ1A-, ß2A-globulin). The progressively changing (longer) half-times observed in turnover studies of normal IgG (7S γ-globulin) may be caused by catabolic heterogeneity of normal 7S immunoglobulins which are immunochemically and catabolically related to γ2a-, γ2b-, and 7S γ1-myeloma proteins. These studies indicate that the 7S γ2a-, 7S γ2b-, and 7S γ1-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 (γ1A-globulin) and probably is independent of IgM (γ1M-globulin). Catabolism of IgA (γ1A-, ß2A-globulin) and IgM (γ1M-globulin) was much more rapid than the catabolism of the 7S γ-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.

Comparative Evaluation of Onion Germplasm (Allium Cepa L.) Of Bangladesh for Physical And Antioxidant Properties

2021 ◽  
Vol 19 (1) ◽  
pp. 113-123
Author(s):  
PK Dash ◽  
S Das ◽  
MA Mannan ◽  
M Jahan
Keyword(s):  
Free Radicals ◽  
Antioxidant Properties ◽  
Biological Properties ◽  
Physicochemical Analysis ◽  
The Other ◽  
Antioxidant Compounds ◽  
Visual Methods ◽  
Ic50 Value ◽  
Onion Germplasm

Determination of antioxidant activity is one of the key elements for understanding the biological properties of a widely used spice onion (A. cepa). In contrast, physical properties help understand the textural quality of onion necessary for postharvest operations of sorting and grading in particular. Considering the physicochemical importance of onion, the present study focused on the determination of physical attributes and antioxidant content of the onion germplasm in Bangladesh using visual methods and 2,2-diphenyl-1-picrylhydrazyl (DPPH) assay, respectively. The five-onion germplasms (BARI Piaz-2, BARI Piaz-3, BARI Piaz-4, BARI Piaz-5, Faridpuri Vati) collected from selected onion growers of the Department of Agricultural Extension (DAE) of the southwestern part of Bangladesh were used as treatments for physicochemical analysis at the Horticulture laboratory of the Agrotechnology Discipline, Khulna University, Khulna, Bangladesh during the period from February to August 2019. The laboratory study was laid out in Completely Randomized Design (CRD) with three replications. Most of the physical characteristics of onion were highest in germplasm-1 than those of the other germplasm tested. The results showed that the DPPH free radicals were scavenged by all onion germplasm extracts in a concentration-dependent pattern. The highest IC50 value (238.10 ppm) was noticed in germplasm-3 and the lowest in germplasm-5 (161.29 ppm) with no statistical difference from germplasm-4 (172.41 ppm). The lower IC50 value indicating that onion germplasms-5 and -4 extracts were more potent in scavenging free radicals than the other onion germplasms. Thus, the low IC50 value facilitated the germplasm-5 and -4 to be enriched with antioxidant compounds significantly in higher amounts than the others. SAARC J. Agric., 19(1): 113-123 (2021)

Comparative Phytochemical Research of Solidago Genus: S. graminifolia. Note I. Flavonoids

2018 ◽  
Vol 1 (1) ◽  
pp. 18-26
Author(s):  
Luciana Dobjanschi ◽  
Ramona Păltinean ◽  
Laurian Vlase ◽  
Mihai Babotă ◽  
Luminita Fritea ◽  
...  
Keyword(s):  
Medicinal Plants ◽  
Quantitative Determination ◽  
Spectrophotometric Method ◽  
Biological Properties ◽  
The Other ◽  
Indigenous Species ◽  
Solidago Canadensis ◽  
Phytochemical Composition ◽  
Chromatographic Profile ◽  
Solidago Virgaurea

Abstract Solidago graminifolia L. Salisb. is one of the latest species appeared in Romania. Due to the interest for the Solidago species as medicinal plants, we researched its phytochemical composition in comparison with the other three species present in Romania: Solidago virgaurea L., Solidago canadensis L., Solidago gigantea Aiton. Starting from the chemotaxonomic value of flavonoids, and their valuable biological properties, we wanted to analyze these substances from S. graminifolia compared to other Solidago species in Romanian flora. The studied species have a high content of flavonoids (3.44-5.21%). The flavonoid substances identified in the indigenous species of Solidago have a high chemotaxonomic value, each species having a charateristic chromatographic profile, therefore their analysis is useful in the case of adulterations. The qualitative analysis of flavonoids was performed by TLC and HPLC-MS, mean while the quantitative determination was achieved by spectrophotometric method and individual fractions separated by HPLC-MS.

scholarly journals IMMUNOLOGICAL STUDIES OF HUMAN γ-GLOBULIN

1960 ◽  
Vol 112 (1) ◽  
pp. 203-223 ◽  
Author(s):  
G. M. Edelman ◽  
J. F. Heremans ◽  
M.-Th. Heremans ◽  
H. G. Kunkel
Keyword(s):  
Deae Cellulose ◽  
Antigenic Determinants ◽  
Agar Diffusion ◽  
Myeloma Proteins ◽  
Zone Electrophoresis ◽  
Γ Globulins

Two major antigenic fragments were obtained from various purified γ-globulin preparations after papain treatment. One, the F component, had a mobility faster than the original γ-globulin and the second, the S component, had a slower mobility. Similar F and S components were also obtained with certain homogeneous myeloma proteins which were closely related to γ-globulin immunologically. Additional minor antigenic components were detected with certain antisera. The technique of immunoelectrophoresis was particularly useful for bringing out the different antigenic constituents obtained after papain treatment. The F and S components as well as a midfraction were isolated by chromatography on DEAE-cellulose. These were immunologically homogeneous and could be utilized to absorb F and S antibodies from various antisera. The relative amount of F and S antibodies varied in different antisera from individual rabbits immunized with whole γ-globulin. Whole γ-globulin was separated by zone electrophoresis into a fast migrating and a more slowly migrating fraction. Each of these gave rise to F and S components after splitting with papain. The F components of the two γ-globulins were similar in mobility, while the S components showed marked mobility differences although antigenically they were very similar. The mobility differences of the parent γ-globulin appeared to be primarily related to the differences in the S component. Certain antisera against pathological γ-globulins were found to give double lines with a wide variety of γ-globulin preparations in agar diffusion. These were shown to be related to the F and S antigenic determinants of γ-glubulin. This relationship was evident by a number of procedures utilizing both Ouchterlony plate techniques and immunoelectrophoresis. The question of whether these findings indicate heterogeneity of γ-globulin in relation to the F and S antigenic components, or whether different antigenic groups on one molecule can give rise to separate lines in certain instances, is discussed.

scholarly journals DEVELOPMENT OF HEPATITIS E 3 GENOTYPE RECOMBINANT PROTEIN CAPSID OF: CLONING, EXPRESSION, PURIFICATION, EVALUATION OF THE ANTIGENIC PROPERTIES

2019 ◽  
Vol 1 (1) ◽  
pp. 10-17 ◽  
Author(s):  
G. I. Alatortseva ◽  
A. V. Sidorov ◽  
L. N. Nesterenko ◽  
L. N. Luhverchik ◽  
V. V. Dotsenko ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Capsid Protein ◽  
Hepatitis E ◽  
Size Exclusion ◽  
Antigenic Specificity ◽  
Clinical Samples ◽  
Genotype 3 ◽  
Recombinant Polypeptide ◽  
Antigenic Properties ◽  
Exclusion Chromatography

Aim. The development of the hepatitis E virus (HEV) genotype 3 recombinant capsid protein.Materials and methods. E.coli strains, plasmid vectors, serological and clinical samples, ELISA reagent kits, molecular biological, bioinformatic, biotechnological, biochemical and serological methods.Results. Using viruscontaining material from pigs of Belgorod region (Russian Federation) we made E.coli strains producing recombinant capsid protein, containing C-terminal of viral ORF2 protein fragment fused to E.coli β-galactosidase. Recombinant protein ORF2 had been isolated from the bacterial inclusion bodies and purified by size exclusion chromatography. Antigenic specificity of the recombinant polypeptide was confirmed by ELISA and Western blotting with sera of hepatitis E patients and reference groups (healthy donors, patients with hepatitis A, B, C, infectious mononucleosis, cytomegalovirus infection and HIV-infected patients). Conclusion. HEV genotype 3 ORF2 recombinant antigen had been developed, and the possibility to use it in diagnostic tests had been experimentally shown.

scholarly journals Transmission of Eurasian avian H2 influenza virus to shorebirds in North America

1999 ◽  
Vol 80 (12) ◽  
pp. 3167-3171 ◽  
Author(s):  
N. V. Makarova ◽  
N. V. Kaverin ◽  
S. Krauss ◽  
D. Senne ◽  
R. G. Webster
Keyword(s):  
North America ◽  
Avian Influenza ◽  
Influenza A ◽  
The Other ◽  
Influenza Surveillance ◽  
Gene Characterization ◽  
Eurasian Lineage ◽  
Antibody Panel ◽  
Antigenic Relationships

Influenza A virus of the H2 subtype caused a serious pandemic in 1957 and may cause similar outbreaks in the future. To assess the evolution and the antigenic relationships of avian influenza H2 viruses, we sequenced the haemagglutinin (HA) genes of H2 isolates from shorebirds, ducks and poultry in North America and derived a phylogenetic tree to establish their interrelationships. This analysis confirmed the divergence of H2 HA into two geographical lineages, American and Eurasian. One group of viruses isolated from shorebirds in North America had HA belonging to the Eurasian lineage, indicating an interregional transmission of the H2 gene. Characterization of HA with a monoclonal antibody panel revealed that the antigenicity of the Delaware strains differed from the other avian strains analysed. The data emphasizes the importance of avian influenza surveillance.

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