scholarly journals An avidin-biotin-peroxidase method for Fc receptors on macrophages isolated from and in sections of rat lung.

1983 ◽  
Vol 31 (9) ◽  
pp. 1139-1141 ◽  
Author(s):  
V M Elner ◽  
A J Hass ◽  
H R Davis ◽  
S Glagov
Keyword(s):  
Immunoglobulin G ◽  
Fc Receptors ◽  
Rat Lung ◽  
Isolated Cells ◽  
Tissue Sections ◽  
Rabbit Immunoglobulin ◽  
Pulmonary Macrophages ◽  
Peroxidase Technique

Receptors for the Fc region of immunoglobulin G (Fc receptors) were detected on pulmonary macrophages by adapting an avidin-biotin-peroxidase technique to isolated cells and sections of rat lung. After incubation with soluble rabbit immunoglobulin G (IgG), surface bound IgG was identified consistently and reproducibly on glass-adherent pulmonary macrophages and on macrophages in tissue sections made from incubated lung slices. Control experiments indicated that binding was specifically mediated by surface Fc receptors. This method may be useful for identifying macrophages in intact tissues.

scholarly journals Human Cytomegalovirus Open Reading Frame TRL11/IRL11 Encodes an Immunoglobulin G Fc-Binding Protein

2001 ◽  
Vol 75 (22) ◽  
pp. 11218-11221 ◽  
Author(s):  
Brendan N. Lilley ◽  
Hidde L. Ploegh ◽  
Rebecca S. Tirabassi
Keyword(s):  
Human Cytomegalovirus ◽  
Immunoglobulin G ◽  
Binding Protein ◽  
Fc Receptors ◽  
Binding Activity ◽  
Open Reading Frame ◽  
Membrane Glycoprotein ◽  
Type I ◽  
Reading Frame

ABSTRACT Several herpesviruses encode Fc receptors that may play a role in preventing antibody-mediated clearance of the virus in vivo. Human cytomegalovirus (HCMV) induces an Fc-binding activity in cells upon infection, but the gene that encodes this Fc-binding protein has not been identified. Here, we demonstrate that the HCMV AD169 open reading frame TRL11 and its identical copy, IRL11, encode a type I membrane glycoprotein that possesses IgG Fc-binding capabilities.

scholarly journals Anti-rabbit immunoglobulin G detection in complex medium by PM-RAIRS and QCM

2007 ◽  
Vol 22 (12) ◽  
pp. 2884-2890 ◽  
Author(s):  
Elisabeth Briand ◽  
Michèle Salmain ◽  
Chantal Compère ◽  
Claire-Marie Pradier
Keyword(s):  
Immunoglobulin G ◽  
Complex Medium ◽  
Rabbit Immunoglobulin

Biology of Human Immunoglobulin G Fc Receptors

1991 ◽  
Vol 49 (5) ◽  
pp. 511-524 ◽  
Author(s):  
Jan G.J. van de Winkel ◽  
Clark L Anderson
Keyword(s):  
Immunoglobulin G ◽  
Fc Receptors ◽  
Human Immunoglobulin ◽  
Human Immunoglobulin G

scholarly journals Differential reduction of interchain disulphide bonds of mouse immunoglobulin G

1968 ◽  
Vol 107 (6) ◽  
pp. 823-828 ◽  
Author(s):  
Alan R. Williamson ◽  
Brigitte A. Askonas
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Polyacrylamide Gel Electrophoresis ◽  
Partial Reduction ◽  
Free Light Chains ◽  
Myeloma Protein ◽  
Heavy Chains ◽  
Disulphide Bonds ◽  
Rabbit Immunoglobulin ◽  
Mouse Immunoglobulin

The relative lability of the interchain disulphide bonds of mouse G2a-myeloma protein 5563 was studied as a function of 2-mercaptoethanol concentration. Analysis of partial-reduction mixtures by polyacrylamide-gel electrophoresis and microdensitometry showed that the disulphide bonds between light and heavy chains are much more susceptible to reduction than the bonds between heavy chains. At a low concentration of 2-mercaptoethanol (10mm) the major dissociable products of mouse immunoglobulin G are heavy-chain dimers and free light chains. These findings contrast with the reported behaviour of rabbit immunoglobulin G, for which the lability of inter-heavy-chain bonds was found to exceed that of the bonds linking light and heavy chains (Hong & Nisonoff, 1965); the relative stability of rabbit immunoglobulin G interchain bonds was confirmed in the present study. Examination of human immunoglobulin G and an immunoglobulin G (γ2) of guinea pig showed that at least in the majority of molecules, as with mouse immunoglobulin G, the disulphide bonds between light and heavy chains are more susceptible to reduction than the inter-heavy-chain bonds.

scholarly journals The disulphide bonds of the heavy chain of rabbit immunoglobulin G

1970 ◽  
Vol 116 (2) ◽  
pp. 261-268 ◽  
Author(s):  
I. J. O'Donnell ◽  
B. Frangione ◽  
R. R. Porter
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Good Yield ◽  
Sequence Variants ◽  
Lower Yield ◽  
Disulphide Bonds ◽  
Rabbit Immunoglobulin ◽  
Minor Sequence

Six peptides containing eight half-cystine residues were isolated in good yield, after either oxidation or reduction and carboxymethylation of fragment C-1, which contains the N-terminal half of the heavy chain of rabbit immunoglobulin G. The sequences of five of these peptides had been reported previously (Cebra, Steiner & Porter, 1968b; Wilkinson, 1969) and that of the sixth was established. Other peptides containing half-cystine residues were isolated in much lower yield and are presumed to be derived from minor sequence variants. The cystine-containing peptides from enzymic digests of whole immunoglobulin G and Fc fraction were studied by several techniques and the results obtained enable us to put forward a scheme of the arrangement of the inter- and intra-chain disulphide bonds.

scholarly journals The subcellular localization of the β-galactoside-binding protein of rat lung

1982 ◽  
Vol 204 (1) ◽  
pp. 97-102 ◽  
Author(s):  
G L Sanford ◽  
L D Davis ◽  
J T Powell
Keyword(s):  
Subcellular Localization ◽  
Immunoglobulin G ◽  
Specific Binding ◽  
Binding Protein ◽  
Rat Lung ◽  
Lectin Activity ◽  
Intracellular Location ◽  
Immature Rat ◽  
Adult Rat ◽  
Rat Lungs

The subcellular localization of the beta-galactoside-binding protein, or lectin, from rat lung was investigated by the specific binding of anti-lectin immunoglobulin G to subcellular fractions. We used both adult and immature (12-day-old) rats; the immature rat lungs have an 8-10-fold greater concentration than adult rat lungs [Powell & Whitney (1980) Biochem. J. 188, 1-8]. In both groups of animals we observed greater specific binding of anti-lectin immunoglobulin G to intracellular membrane (mitochondrial and microsomal fractions) than to plasma membranes. Pre-incubation of membrane fractions with lactose resulted in a marked diminution of anti-lectin immunoglobulin G binding. In the adult rat lung most (approx. 80%) of the lectin activity was membrane-associated. In the immature rat lung only approx. 30% of the lectin activity was membrane associated and most of the beta-galactoside-binding protein appeared to be a soluble cytoplasmic component. The rat lung beta-galactoside-binding protein appeared to have a broad but predominantly intracellular location, being associated with membranes through one of its galactoside-binding sites.

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