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Concanavalin A Reaction with Human Normal Immunoglobulin G and Myeloma Immunoglobulin G
Science, 1967Concanavalin 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.
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Fragmentation of Immunoglobulin
AbstractThis unit describes procedures for fragmentation of IgG to the monovalent Fab fragment using papain digestion, and to the bivalent F(ab′)2 fragment by pepsin digestion. Alternative methods of fragmentation to F(ab′)2 include use of papain that is preactivated with cysteine and use of the enzyme ficin.
Sarah M, Andrew, Julie A, Titus
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The carbohydrate composition of immunoglobulins G
Biochimica et Biophysica Acta (BBA) - General Subjects, 1971Abstract 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.
W, Niedermeier +3 more
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Significance of immunoglobulin G subclasses
The American Journal of Medicine, 1984IgG 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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Immunoglobulin G Glycosylation in Diseases
2021Changes in immunoglobulin G (IgG) glycosylation pattern have been observed in a vast array of auto- and alloimmune, infectious, cardiometabolic, malignant, and other diseases. This chapter contains an updated catalog of over 140 studies within which IgG glycosylation analysis was performed in a disease setting.
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Purification of Immunoglobulin G (IgG)
2003Several 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.
M G, Baines, R, Thorpe
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Placental transport of immunoglobulin G
Vaccine, 2003Maternal 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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