Results 221 to 230 of about 620,586 (241)
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In vitro glycation of human immunoglobulin G
Clinica Chimica Acta, 2004Glucose can covalently bind to the proteins by nonenzymatic process often termed glycation. Glycation of IgG is of special interest due to its possible influence on the functionality of immunoglobulins and overall immunocompetence.The glycation of IgG was studied using radioactive D-[U-14C]-glucose.The kinetics, concentration/temperature dependence and
Mirjana Šimić +4 more
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Cancer, 1991
Persistent low serum levels of one or several immunoglobulin G (IgG) subclasses can be found in a high proportion of adult patients with increased susceptibility to infections. It is hard to envision that the low subclass level in itself is responsible for this susceptibility because healthy blood donors have been described who are completely devoid of
A. Enskog +2 more
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Persistent low serum levels of one or several immunoglobulin G (IgG) subclasses can be found in a high proportion of adult patients with increased susceptibility to infections. It is hard to envision that the low subclass level in itself is responsible for this susceptibility because healthy blood donors have been described who are completely devoid of
A. Enskog +2 more
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Infection and Immunity, 1979
The role of immunoglobulin G (IgG) as an opsonin in phagocytosis of Cryptococcus neoformans by macrophages was investigated. Labeling with 125I showed that IgG isolated from normal human serum bound to non-encapsulated C. neoformans. Furthermore, IgG-opsonized cryptococci were agglutinated by anti-serum to IgG heavy chains, indicating that normal human
T R Kozel, T G McGaw
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The role of immunoglobulin G (IgG) as an opsonin in phagocytosis of Cryptococcus neoformans by macrophages was investigated. Labeling with 125I showed that IgG isolated from normal human serum bound to non-encapsulated C. neoformans. Furthermore, IgG-opsonized cryptococci were agglutinated by anti-serum to IgG heavy chains, indicating that normal human
T R Kozel, T G McGaw
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Colloids and Surfaces, 1984
Abstract The spatial complementarity between antigen and antibody is the major prerequisite for antigen—antibody interaction. This interaction was investigated using a model system with oriented lipid A in a monolayer on the air—water interface and homologous IgG antibody in the substrate. Two immunoglobulins were employed, i.e., specific IgG (s-IgG)
Ivan Panaiotov +5 more
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Abstract The spatial complementarity between antigen and antibody is the major prerequisite for antigen—antibody interaction. This interaction was investigated using a model system with oriented lipid A in a monolayer on the air—water interface and homologous IgG antibody in the substrate. Two immunoglobulins were employed, i.e., specific IgG (s-IgG)
Ivan Panaiotov +5 more
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Colloids and Surfaces, 1986
Abstract A mixed spread monolayer composed of antigen and homologous antibody served as a model of lipid A—antilipid A IgG interaction at the air—water interface. Its behaviour was compared with that of lipid A—normal IgG. The immunoglobulins used were antilipid A IgG (s-IgG) and normal IgG (n-IgG).
R. Ivanova +4 more
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Abstract A mixed spread monolayer composed of antigen and homologous antibody served as a model of lipid A—antilipid A IgG interaction at the air—water interface. Its behaviour was compared with that of lipid A—normal IgG. The immunoglobulins used were antilipid A IgG (s-IgG) and normal IgG (n-IgG).
R. Ivanova +4 more
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Immunoglobulin G subclasses in wheezing infants
Pediatrics International, 1998Abstract Background: The wheezing infant is a common but difficult patient to approach diagnostically. The prevalence of immunoglobulin (Ig) G subclass deficiency in wheezing infants is still controversial. Methods: We studied the serum concentration of IgG subclasses in 38 wheezing infants (aged6–24 ...
Uzuner, N, Uguz, A, Karaman, O
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Identification of immunoglobulin G in the vitreous of rabbits
Experimental Eye Research, 1968Antigenic determinants of immunoglobulin G were identified in the vitreous of the rabbit by use of specific immunological methods and were shown to be derived from the maternal circulation. It was demonstrated that with increasing age there is a diminution in concentration of this protein in the eye.
Ralph J. Helmsen, Rose G. Mage
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Degradation of immunoglobulin G by periodontal bacteria
Oral Microbiology and Immunology, 1994Several subgingival microorganisms were tested for their ability to utilize human immunoglobulin G (IgG) as a substrate for growth. This was done using a protein‐free chemically defined medium, supplemented with IgG. Stimulation of growth was observed for Capnocytophaga ochracea, Porphyromonas asaccharolytica, Porphyromonas endodontalis, Porphyromonas ...
J. A. J. M. Bakkeren +5 more
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Immunoglobulin G immobilization on PVDF surface
Colloids and Surfaces B: Biointerfaces, 2014Immobilization of antibody molecules onto hydrophobic polymeric surfaces with disordered orientation is something unwanted in many applications. To overcome this drawback, controlled immunoglobulin G (IgG) immobilization onto poly(vinylidene fluoride) surface was investigated in this paper.
Elena Pâslaru +5 more
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Interaction of C3 and C3b with immunoglobulin G
Molecular Immunology, 1983Human C3b as well as native C3 were found to bind to solid phase human and rabbit IgG. Haemolytically active C3 had significantly higher binding capacity to IgG than the C3b fragment. Inhibition experiments proved that C3 and C3b have common binding sites on the Fab and Fc part of the IgG molecule but the character of these binding sites was different.
János Gergely +3 more
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