scholarly journals A Monosaccharide Residue Is Sufficient to Maintain Mouse and Human IgG Subclass Activity and Directs IgG Effector Functions to Cellular Fc Receptors

Cell Reports ◽  
2015 ◽  
Vol 13 (11) ◽  
pp. 2376-2385 ◽  
Author(s):  
Daniela Kao ◽  
Heike Danzer ◽  
Mattias Collin ◽  
Andrea Groß ◽  
Jutta Eichler ◽  
...  
Keyword(s):  
Fc Receptors ◽  
Igg Subclass ◽  
Monosaccharide Residue ◽  
Human Igg ◽  
Effector Functions

Human IgG Fc Receptors

1997 ◽  
Vol 16 (1-2) ◽  
pp. 29-55 ◽  
Author(s):  
Ingmar A. F. M. Heijnen ◽  
Jan G. J. Van de Winkel
Keyword(s):  
Fc Receptors ◽  
Human Igg

ELISA detection of human IgG subclass antibodies to Streptococcus mutans

1986 ◽  
Vol 87 (1) ◽  
pp. 95-102 ◽  
Author(s):  
S.J. Challacombe ◽  
M. Biggerstaff ◽  
C. Greenall ◽  
D.M. Kemeny
Keyword(s):  
Streptococcus Mutans ◽  
Igg Subclass ◽  
Human Igg

An Enzyme-Linked Immunosorbent Assay (Elisa) for Measurement of Human Igg Subclass Levels in Serum

1990 ◽  
Vol 23 (6) ◽  
pp. 1017-1037 ◽  
Author(s):  
Kunihiko Hayashi ◽  
Hiroshi Miyasaka ◽  
Munekazu Tagawa
Keyword(s):  
Immunosorbent Assay ◽  
Enzyme Linked Immunosorbent Assay ◽  
Igg Subclass ◽  
Human Igg

scholarly journals Rubella-specific IgG subclass concentrations in sera using an enzyme-linked immunosorbent assay (ELISA): the effect of different sources of rubella antigen

1988 ◽  
Vol 101 (3) ◽  
pp. 599-604 ◽  
Author(s):  
H. I. J Thomas ◽  
P. Morgan-Capner
Keyword(s):  
Immunosorbent Assay ◽  
Enzyme Linked Immunosorbent Assay ◽  
Igg Subclass ◽  
Human Igg ◽  
Discrepant Result ◽  
Specific Igg ◽  
Antigen A ◽  
Different Sources ◽  
Positive Results

SUMMARYFive rubella antigens were evaluated in an antiglobulin enzyme-linked immunosorbent assay for rubella-specific IgG subclass antibody. One monoclonal anti-human IgG subclass antibody was used for each of IgG1, IgG2and IgG4, but two were compared for IgG3. A total of 101 sera were tested from cases of rubella in the distant past and from cases of primary rubella, reinfection and following immunization. Only one serum gave a discrepant result for specific IgG1, being positive with only one rubella antigen, a commercially prepared antigen coated on to microtitre wells (Enzygnost; Behringwerke). No sera contained detectable specific IgG2. Only four sera contained specific IgG4, and this was detectable only with Enzygnost antigen. For specific IgG3little difference was observed between the two monoclonal anti-human IgG3subclass antibodies; only two very weakly positive sera gave discrepant results. However, varying results were obtained for specific IgG3with the different antigens. Enzygnost gave more positive results for specific IgG3with most categories of sera.It is concluded that the differences between various reports of the rubella-specific IgG subclass profile cannot be explained entirely by the use of different rubella antigens.

Immunochemical Characterisation Of Two Human Factor IX Inhibitors And Treatment With Activated Concentrate

1981 ◽  
Author(s):  
J C Giddings ◽  
A L Bloom
Keyword(s):  
Exchange Chromatography ◽  
Factor Ix ◽  
Therapeutic Trial ◽  
Igg Subclass ◽  
Human Igg ◽  
Heavy Chains ◽  
Human Factor Ix ◽  
Activity Unit ◽  
Factor Ix Deficiency

Plasma was obtained from two unrelated patients (A and B) with severe hereditary factor IX deficiency who had developed specific inhibitors of factor IX. Immunoglobulin (Ig) was fractionated by salt precipitation and ion exchange chromatography and resulted in 90% recovery of the factor IX inhibitor. Inhibitor plasma or Ig fractions were mixed with specific antisera to ig chains, incubated and centrifuged. Supernatant was assayed for residual inhibitor. Antisera, specific for the heavy chains of human IgG, IgA, IgM, IgD and IgE and the subclasses 1 to 4 of human IgG were used together with antisera specific for the kappa and lambda light chains of IgG. Results of inhibitor neutralisation assays were the same whether plasma or Ig fractions were used. Inhibitor from patient A was completely neutralised by anti IgG and by anti-lambda serum, and was largely neutralised by antiserum to IgG subclass 4. Other antisera had no effect. Inhibitor from patient B was completely neutralised by anti IgG and partially neutralised by anti-kappa and anti-lambda serum. Partial neutralisation of inhibitor was also seen with antisera to IgG subclass 1 and IgG subclass 4. Other antisera again had no effect. Inhibitor A inactivated factor IX instantaneously to a titre of 1 in 100. Neither conventional factor IX concentrate (Oxford DE) at 1 u/ml nor activated‘factor IX’ concentrate (Feiba, Immuno) at 1 u/ml (‘activity’ unit) corrected the kaolin cephalin clotting time (KCCT) of patient A in vitro. However after intravenous administration of Feiba (25 u/kg) progressive shortening of the KCCT occurred from 127 sec. to 60 sec. at 60 min. and was followed by rapid resolution of a haemarthrosis. It is concluded that factor IX antibodies may be of monoclonal or oligoclonal immunoglobulin class and that on development, therapeutic trial of activated factor IX-prothrombin concentrates is indicated for the control of bleeding.

Human IgG subclass assays using a novel assay method

1986 ◽  
Vol 88 (1) ◽  
pp. 65-73 ◽  
Author(s):  
Joseph Mayus ◽  
Kim Macke ◽  
Penelope Shackelford ◽  
Jerry Kim ◽  
Moon Nahm
Keyword(s):  
Assay Method ◽  
Igg Subclass ◽  
Human Igg

Molecular definition of interaction sites on human IgG for Fc receptors (huFcγR)

1990 ◽  
Vol 27 (12) ◽  
pp. 1237-1240 ◽  
Author(s):  
Royston Jefferis ◽  
John Lund ◽  
John Pound
Keyword(s):  
Fc Receptors ◽  
Human Igg ◽  
Interaction Sites ◽  
Definition Of

scholarly journals Unexplained Abuses of Human IgG Subclass Denomination in Antibody Patents

BioDrugs ◽  
2014 ◽  
Vol 28 (4) ◽  
pp. 327-329
Author(s):  
Jérémy Pottier ◽  
Hervé Watier
Keyword(s):  
Igg Subclass ◽  
Human Igg

scholarly journals A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins

1990 ◽  
Vol 268 (3) ◽  
pp. 529-537 ◽  
Author(s):  
R Jefferis ◽  
J Lund ◽  
H Mizutani ◽  
H Nakagawa ◽  
Y Kawazoe ◽  
...  
Keyword(s):  
Comparative Study ◽  
Internal Space ◽  
Igg Subclass ◽  
Human Igg ◽  
Polyclonal Igg ◽  
Oligosaccharide Structures

Quantitative oligosaccharide profiles were determined for each of 18 human IgG paraproteins representing the four subclasses. Each paraprotein exhibits a unique profile that may be substantially different from that observed for polyclonal IgG. The IgG2 and some IgG3 proteins analysed exhibit a predominance of oligosaccharide moieties having galactose on the Man(alpha 1----3) arm rather than the Man(alpha 1----6) arm; it was previously held that galactosylation of the Man(alpha 1----6) arm is preferred, as observed for IgG1, IgG4 and polyclonal IgG. An IgG4 protein is reported that has galactosylated Man(alpha 1----3) and Man(alpha 1----6) arms on both Fc-localized carbohydrate moieties; previous findings suggested that such fully glycosylated structures could not be accommodated within the internal space of the C gamma 2 domains. Unusual monoantennary oligosaccharides present in IgG2 and IgG3 proteins were isolated and their structures determined.

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