Results 251 to 260 of about 243,158 (289)
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Purification of Immunoglobulin G
Current Protocols in Cell Biology, 1997AbstractWhile unpurified antibodies are suitable for a number of applications, purified antibodies are required for assays based on known concentration of antibody, for chemical modifications such as radiolabeling or conjugation with fluorochromes, or for structural modifications such as production of F(ab')2 or monvalent Fab fragments.
Julie A. Titus, Sarah M. Andrew
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The interactions of calreticulin with immunoglobulin G and immunoglobulin Y
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2011Calreticulin is a chaperone of the endoplasmic reticulum (ER) assisting proteins in achieving the correctly folded structure. Details of the binding specificity of calreticulin are still a matter of debate. Calreticulin has been described as an oligosaccharide-binding chaperone but data are also accumulating in support of calreticulin as a polypeptide ...
Møllegaard, Karen Mai +9 more
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The human placental immunoglobulin G receptor and immunoglobulin G transport
American Journal of Obstetrics and Gynecology, 1994The objective of this study was to quantitatively determine an immunoglobulin G receptor, placental alkaline phosphatase, and its ligand immunoglobulin G in maternal and fetal blood and to study the transport capacity of the receptor.Venous blood samples from 66 term pregnant women and cord samples from their fetuses were obtained, together with the ...
Barbro E. Fridén +4 more
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Epigenetics of Immunoglobulin G Glycosylation
2021Alternative glycosylation of immunoglobulin G (IgG) affects its effector functions during the immune response. IgG glycosylation is altered in many diseases, but also during a healthy life of an individual. Currently, there is limited knowledge of factors that alter IgG glycosylation in the healthy state and factors involved in specific IgG ...
Marija Klasić, Vlatka Zoldoš
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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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Secretory immunoglobulin A and immunoglobulin G in horse saliva
Veterinary Immunology and Immunopathology, 2016This study aimed to increase the knowledge on salivary antibodies in the horse since these constitute an important part of the immune defence of the oral cavity. For that purpose assays to detect horse immunoglobulin A (IgA) including secretory IgA (SIgA) were set up and the molecular weights of different components of the horse IgA system were ...
Eva Wattrang +4 more
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Immunoglobulins: Structural Studies of Immunoglobulin G
Nature, 1969In the following three articles, details are given of the structure and chemical typing of immunoglobulins.
J. R. L. Pink, C. Milstein, B. Frangione
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Immunoglobulin G Subclass Deficiencies
International Archives of Allergy and Immunology, 1987Low levels of single or multiple serum immunoglobulin G (IgG) subclasses is a common finding among patients with increased susceptibility to infections. In this investigation we summarize data from studies of 503 subclass-deficient individuals. Low IgG2 levels was the most common deficiency among children, and boys were more often deficient than girls.
R. Söderström +5 more
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1985
Publisher Summary This chapter provides an overview of immunoglobulin G (IgG). IgG molecules consist of identical pairs of heavy (H) and light (L) chains (MW = 50,000 and 25,000, respectively) linked by disulfide bridges. A proteolytic enzyme (papain) splits IgG into three fragments which retain biological activity: two Fab (for antigen binding ...
Peter D. Gorevic +2 more
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Publisher Summary This chapter provides an overview of immunoglobulin G (IgG). IgG molecules consist of identical pairs of heavy (H) and light (L) chains (MW = 50,000 and 25,000, respectively) linked by disulfide bridges. A proteolytic enzyme (papain) splits IgG into three fragments which retain biological activity: two Fab (for antigen binding ...
Peter D. Gorevic +2 more
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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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