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Immunoglobulin G in the Rabbit Cornea

Archives of Ophthalmology, 1969
Immunoglobulin G was detected by the fluorescent antibody technique in the corneas of six rabbits. It was present throughout the stroma and was not present in the epithelium, in Descemet's membrane, or in the endothelium.
Mathea R. Allansmith   +2 more
openaire   +3 more sources

Purification of Immunoglobulin G (IgG)

2003
Several immunological procedures can be successfully carried out using nonpurified antibodies, such as unfractionated antisera, or ascitic fluid/culture supernatant containing monoclonal antibodies (MAbs). However, a much "cleaner" result can often be obtained if some form of enrichment or isolation of immunoglobulin is employed.
Robin Thorpe, Michael G. Baines
openaire   +4 more sources

The carbohydrate composition of immunoglobulins G

Biochimica et Biophysica Acta (BBA) - General Subjects, 1971
Abstract Immunoglobulin G from human, horse, sheep, pig, cow, chicken, rabbit and dog blood serum was analyzed for its carbohydrate composition by gas chromatography, using alditol acetate derivatives of sugars released by acid hydrolysis. Fucose, mannose, galactose, glucosamine and sialic acid were present in IgG of all species studied.
T Kirkland   +3 more
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Concanavalin A Reaction with Human Normal Immunoglobulin G and Myeloma Immunoglobulin G

Science, 1967
Concanavalin A precipitated less than 5 percent of immunoglobulin G from human serum. It reacted with all of 42 myeloma serums of the immunoglobulin G type tested, but no more than approximately 50 percent of the total myeloma protein was ever precipitated.
openaire   +3 more sources

Human Immunoglobulin G and Immunoglobulin G Subclasses: Biochemical, Genetic, and Clinical Aspects

Critical Reviews in Clinical Laboratory Sciences, 1989
Human IgG consists of two identical heavy (H) chains and two identical light (L) chains joined by interchain disulfide bridges. Heterogeneity in the amino acid sequences of the H and L polypeptides results in at least three types of IgG variants at the structural and genetic levels.
Irene J. Check, Christine Papadea
openaire   +3 more sources

Significance of immunoglobulin G subclasses

The American Journal of Medicine, 1984
IgG subclasses differ from one another both immunochemically and functionally. An isolated absence of a certain specific subclass may or may not be associated with disease. However, an absence of serum IgG4 as measured by a sensitive radioimmunoassay is usually, if not always, associated with severe recurrent pyogenic infections, usually of the ...
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Serum immunoglobulins and immunoglobulin G subclasses with recurrent wheezing

The Indian Journal of Pediatrics, 2000
In this study serum immunoglobulins (Ig) and IgG subclasses were measured in 42 patients (ranging 9 month-6 year) with recurrent wheezing and in 37 healthy children determined the relationship between serum Igs and recurrent wheezing. Patients were divided into two groups according to the age [9 month-2 year (n: 15), and 2-6 year (n: 27)].
Ahment Faik Öner   +5 more
openaire   +3 more sources

Placental transport of immunoglobulin G

Vaccine, 2003
Maternal antibodies transported across the placenta protect the newborn. Maternal immunoglobulin G (IgG) concentrations in fetal blood increase from early in the second trimester through term, most antibodies being acquired during the third trimester. IgG1 is the most efficiently transported subclass and IgG2 the least.
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Immunoglobulin subclasses and prophylactic use of immunoglobulin in immunoglobulin g subclass deficiency

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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In vitro glycation of human immunoglobulin G

Clinica Chimica Acta, 2004
Glucose 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
openaire   +3 more sources

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