Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The oligosaccharide units of rabbit immunoglobulin G. Asymmetric attachment of C2-oligosaccharide.

ABSTRACT: Two populations of immunoglobulin G (IgG) molecules were isolated from pooled rabbit serum. The first was almost devoid of galactosamine and was obtained in a yield of 7% of the total IgG; the second contained on average a single residue of galactosamine per molecule and was obtained in a yield of 30% of the total IgG. The galactosamine, which is present solely in the C2-oligosaccharide, appeared to be present on one H-chain and not the other in the four-chain structure. Evidence was obtained by the isolation of a glycopeptide linked through a disulphide bridge to a second peptide of the same sequence; the oligosaccharide attached to the first peptide was absent from the complementary peptide. Further evidence was obtained by degradation and analysis of the 5S IgG fragment, which comprises an intact half-molecule coupled through a disulphide bridge to the Fc fragment derived from the opposing half molecule (Goodman, 1965); only the intact H-chain carried the C2-oligosaccharide.

SUBMITTER: Fanger MW

PROVIDER: S-EPMC1178786 | biostudies-other | 1972 May

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

The oligosaccharide units of rabbit immunoglobulin G. Multiple carbohydrate attachment sites.

Project description:The carbohydrate structure of rabbit immunoglobulin G isolated from pooled sera was investigated. Amino sugar analysis of fragments of the molecule allowed three oligosaccharides to be located at separate sites on the H-chain. The corresponding glycopeptides were isolated. The average composition of the C1-oligosaccharide was 2 glucosamine, 1 mannose and 2 galactose residues. It appeared to be present in approx. 15% of the H-chains; the carbohydrate was coupled through the amide group of asparagine in a peptide containing asparagine, glycine and threonine within the Fd fragment of the molecule. The average composition of the C2-oligosaccharide was 1 galactosamine, 1 galactose and either 1 or 2 sialic acid residues. It was present on approx. 40% of the H-chains and was attached glycosidically to the OH group of threonine in a peptide Ser-Lys-Pro-Thr-Cys-Pro-Pro-Glu-Leu in the hinge region of the molecule. The average composition of the C3-oligosaccharide was 5 glucosamine, 2 galactose, 5 mannose, 1 fucose and 1 sialic acid residue. It appeared to be present in all the H-chains and was linked through the amide group of asparagine in a peptide Gln-Gln-Phe-Asn-Ser-Thr-Ile-Arg within the Fc fragment of the molecule.

| S-EPMC1178785 | biostudies-other

The oligosaccharide units of a human type L immunoglobulin M (Macroglobulin).

Project description:1. The carbohydrate composition of the monomeric unit of a type L macroglobulin (immunoglobulin M) was determined as 6 residues of fucose, 35 of mannose, 11 of galactose, 27 of N-acetylglucosamine and 9 of sialic acid. 2. Two types of oligosaccharide unit were present in the protein, one of which (Ca type) contained fucose, mannose, galactose, N-acetylglucosamine and sialic acid in the molar proportions 1:3-4:2:3-5:0-2, and the other (Cb type) contained mannose and N-acetylglucosamine in the proportions 6-8:2-3. 3. A tentative structure is proposed for the Cb type unit. 4. An S-carboxymethylcysteine-containing glycopeptide with a Ca-type unit was isolated after reduction, alkylation and tryptic digestion of the protein. 5. The immunoglobulin monomer appears to contain six oligosaccharide units of the Ca type and two of the Cb type.

| S-EPMC1177075 | biostudies-other

Chiral C2-Symmetric Diimines with 4,5-Diazafluorene Units.

Project description:A synthetic approach to a new group of stable chiral C2-symmetric diimines with the 4,5-diazafluorene core has been developed based on condensation of dipinodiazafluorene with aromatic diamines. The chemical structures of new compounds were proven by spectroscopic methods and X-ray crystallography. All the compounds form solvates with organic solvents (chloroform, benzene, 1,4-dioxane) and water. Specific spectral data of the new compounds are explained using calculated data (DFT). Diimines of the pinodiazafluorene series give colored reactions with transition metal ions and can be regarded as prospective polydentate ligands with interesting luminescent and chiroptical properties.

| S-EPMC6749561 | biostudies-literature

Investigations on the oligosaccharide units of an A myeloma globulin.

Project description:The carbohydrate content of an A myeloma globulin was investigated. The carbohydrate content was found to be unchanged when the protein was isolated from the patient over a period of 18 months. The various polymeric forms of the protein contained similar proportions of carbohydrate. The A myeloma globulin contained approx. 2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains. The oligosaccharide units showed two kinds of heterogeneity, which have been termed central and peripheral. Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2). The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid. Tentative structures are proposed for these various types of oligosaccharide unit. Glycopeptides were isolated in which the sialic acid content exceeded that of d-galactose. Explanations are given for the electrophoretic mobility and staining characteristics of the various glycopeptides.

| S-EPMC1198669 | biostudies-other

Systematic characterization and comparative analysis of the rabbit immunoglobulin repertoire.

Project description:Rabbits have been used extensively as a model system for the elucidation of the mechanism of immunoglobulin diversification and for the production of antibodies. We employed Next Generation Sequencing to analyze Ig germline V and J gene usage, CDR3 length and amino acid composition, and gene conversion frequencies within the functional (transcribed) IgG repertoire of the New Zealand white rabbit (Oryctolagus cuniculus). Several previously unannotated rabbit heavy chain variable (VH) and light chain variable (VL) germline elements were deduced bioinformatically using multidimensional scaling and k-means clustering methods. We estimated the gene conversion frequency in the rabbit at 23% of IgG sequences with a mean gene conversion tract length of 59±36 bp. Sequencing and gene conversion analysis of the chicken, human, and mouse repertoires revealed that gene conversion occurs much more extensively in the chicken (frequency 70%, tract length 79±57 bp), was observed to a small, yet statistically significant extent in humans, but was virtually absent in mice.

| S-EPMC4076286 | biostudies-literature

Efficient immunoglobulin gene disruption and targeted replacement in rabbit using zinc finger nucleases.

Project description:Rabbits are widely used in biomedical research, yet techniques for their precise genetic modification are lacking. We demonstrate that zinc finger nucleases (ZFNs) introduced into fertilized oocytes can inactivate a chosen gene by mutagenesis and also mediate precise homologous recombination with a DNA gene-targeting vector to achieve the first gene knockout and targeted sequence replacement in rabbits. Two ZFN pairs were designed that target the rabbit immunoglobulin M (IgM) locus within exons 1 and 2. ZFN mRNAs were microinjected into pronuclear stage fertilized oocytes. Founder animals carrying distinct mutated IgM alleles were identified and bred to produce offspring. Functional knockout of the immunoglobulin heavy chain locus was confirmed by serum IgM and IgG deficiency and lack of IgM(+) and IgG(+) B lymphocytes. We then tested whether ZFN expression would enable efficient targeted sequence replacement in rabbit oocytes. ZFN mRNA was co-injected with a linear DNA vector designed to replace exon 1 of the IgM locus with ?1.9 kb of novel sequence. Double strand break induced targeted replacement occurred in up to 17% of embryos and in 18% of fetuses analyzed. Two major goals have been achieved. First, inactivation of the endogenous IgM locus, which is an essential step for the production of therapeutic human polyclonal antibodies in the rabbit. Second, establishing efficient targeted gene manipulation and homologous recombination in a refractory animal species. ZFN mediated genetic engineering in the rabbit and other mammals opens new avenues of experimentation in immunology and many other research fields.

| S-EPMC3113902 | biostudies-literature

Proteolysis of rabbit immunoglobulin M by papain.

Project description:1. Digestion of rabbit immunoglobulin M (IgM) by papain for 5h, in the absence of reducing agent, gives Fabmu and Fc(5)mu fragments in high yield. Shorter periods give fragment Fc(5)mu with one or more Fabmu fragments still attached. 2. Reducing agent in the absence of a denaturant cleaves rabbit IgM into half-subunits, each containing one mu chain and one light chain. Digestion by papain in the presence of such a reducing agent destroys the Fcmu domains.

| S-EPMC1168411 | biostudies-other

Printable magnesium ion quasi-solid-state asymmetric supercapacitors for flexible solar-charging integrated units.

Project description:Wearable and portable self-powered units have stimulated considerable attention in both the scientific and technological realms. However, their innovative development is still limited by inefficient bulky connections between functional modules, incompatible energy storage systems with poor cycling stability, and real safety concerns. Herein, we demonstrate a flexible solar-charging integrated unit based on the design of printed magnesium ion aqueous asymmetric supercapacitors. This power unit exhibits excellent mechanical robustness, high photo-charging cycling stability (98.7% capacitance retention after 100 cycles), excellent overall energy conversion and storage efficiency (?overall?=?17.57%), and outstanding input current tolerance. In addition, the Mg ion quasi-solid-state asymmetric supercapacitors show high energy density up to 13.1 mWh cm-3 via pseudocapacitive ion storage as investigated by an operando X-ray diffraction technique. The findings pave a practical route toward the design of future self-powered systems affording favorable safety, long life, and high energy.

| S-EPMC6820525 | biostudies-literature

Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway.

Project description:Fifty years ago, Kornberg and Krebs established the glyoxylate cycle as the pathway for the synthesis of cell constituents from C2-units. However, since then, many bacteria have been described that do not contain isocitrate lyase, the key enzyme of this pathway. Here, a pathway termed the ethylmalonyl-CoA pathway operating in such organisms is described. Isotopically labeled acetate and bicarbonate were transformed to ethylmalonyl-CoA by cell extracts of acetate-grown, isocitrate lyase-negative Rhodobacter sphaeroides as determined by NMR spectroscopy. Crotonyl-CoA carboxylase/reductase, catalyzing crotonyl-CoA + CO2 + NADPH --> ethylmalonyl-CoA- + NADP+ was identified as the key enzyme of the ethylmalonyl-CoA pathway. The reductive carboxylation of an enoyl-thioester is a unique biochemical reaction, unprecedented in biology. The enzyme from R. sphaeroides was heterologously produced in Escherichia coli and characterized. Crotonyl-CoA carboxylase/reductase (or its gene) can be used as a marker for the presence of the ethylmalonyl-CoA pathway, which functions not only in acetyl-CoA assimilation. In Streptomyces sp., it may also supply precursors (ethylmalonyl-CoA) for antibiotic biosynthesis. For methylotrophic bacteria such as Methylobacterium extorquens, extension of the serine cycle with reactions of the ethylmalonyl-CoA pathway leads to a simplified scheme for isocitrate lyase-independent C1 assimilation.

| S-EPMC1965564 | biostudies-other

Fifty-million-year-old polymorphism at an immunoglobulin variable region gene locus in the rabbit evolutionary lineage.

Project description:The Ig heavy chain variable region (V(H)) genes encode the antigen-binding regions of antibodies. The rabbit genome contains more than 100 V(H) genes, but only one (V(H)1) is preferentially used in the VDJ gene rearrangement. Three highly divergent alleles occur at this V(H)1 locus in most rabbit populations. These three V(H) alleles are also present in snowshoe hare populations, indicating that the polymorphism of the V(H)1 alleles is trans-specific. Here we report the results of a phylogenetic analysis of rabbit Ig germ-line V(H) genes (alleles) together with V(H) genes from humans and mice. We have found that all rabbit V(H) genes belong to one mammalian V(H) group (group C), which also includes various human and mouse V(H) genes. Using the rate of nucleotide substitution obtained from human and mouse V(H) sequences, we have estimated that the V(H)1 polymorphism in the rabbit lineage has been maintained for about 50 million years. This extremely long persistence of V(H)1 polymorphism is apparently caused by overdominant selection, though the real mechanism is unclear.

| S-EPMC22275 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data