4 edition of Carbohydrate moieties of immunoglobulin found in the catalog.
|Statement||papers by Harold C. Sox [and others]|
|Contributions||Sox, Harold C.|
|LC Classifications||QR186.7 .C37|
|The Physical Object|
|Number of Pages||187|
|LC Control Number||74003461|
Carbohydrate Moieties of Microsporidian Polar Tube Proteins Are Targeted by Immunoglobulin G in Immunocompetent Individuals Ron Peek,1* Fre´de´ric Delbac,2 Dave Speijer,3 Vale´rie Polonais,2 Sophie Greve,1 Ellen Wentink-Bonnema,1 Jeffrey Ringrose,4 and Tom van Gool1,5Cited by: Despite the paradigm that carbohydrates are T cell–independent antigens, isotype-switched glycan-specific immunoglobulin G (IgG) antibodies and polysaccharide-specific T cells are found in humans. We used a systems-level approach combined with glycan array technology to decipher the repertoire of carbohydrate-specific IgG antibodies in intravenous and subcutaneous immunoglobulin Cited by:
To establish the method for glycopeptide synthesis using glycosylated amino acids whose carbohydrate moieties are protected with an acid-labile protecting group, we synthesized O-Boc-protected glycosylated amino acids (GlcNAc-Asn and Man-Thr).At first, we synthesized GlcNAc-Asn derivative 1 as a building block for N-linked glycopeptide shown in Chart 2, the hydroxyl groups of Author: Tomohiro Tanaka, Mika Shiraishi, Akio Matsuda, Mamoru Mizuno. CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): The subcellular sites of synthesis and route of intracellular transfer of immunoglobulin G (IgG) have been investigated by electron microscope radioautography with precursors used for the polypeptide chain (leucine-'H) and for the carbohydrate moieties (galactose 3H and glucosamine-'H).
The subcellular sites of synthesis and route of intracellular transfer of immunoglobulin G (IgG) have been investigated by electron microscope radioautography with precursors used for the polypeptide chain (leucine-3 H) and for the carbohydrate moieties (galactose-3 H and glucosamine-3 H).For this purpose, plasma cells from a mouse myeloma tumor were labeled with appropriate . ROLE OF CARBOHYDRATE RESIDUES IN IMMUNOGLOBULIN BIOCHEMISTRY (Moscow) Vol. 81 No. 8 membranes. Following synthesis the IgG molecules, they are pinocyted by endothelial cells that bind with high affinity (K D ≈10 nM) to histidine residues of the bindingFile Size: 5MB.
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Carbohydrate moieties of immunoglobulin. New York, MSS Information Corp.  (OCoLC) Online version: Carbohydrate moieties of immunoglobulin. New York, MSS Information Corp.
 (OCoLC) Document Type: Book: All Authors /. Full text Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (K), or click on a Carbohydrate moieties of immunoglobulin book image below to browse page by page.
Links to PubMed are also available for Selected by: 4. A novel method is described for the biotinylation of immunoglobulins. The procedure relies on the generation of reactive aldehydes on the carbohydrate moieties of the immunoglobulin by oxidation with sodium periodate and subsequent reaction with biotin by: Biosynthesis of the carbohydrate portion of immunoglobulin radiochemical and chemical analysis of the carbohydrate moieties of two myeloma proteins purified from different subcellular fractions of plasma cells.
Fritz Melchers. Biochemistry,10 (4), pp – DOI: /bia Comparative study of the carbohydrate moieties of normal and pathological human immunoglobulins M Article (PDF Available) in Biochemical Journal (1) May with 20 Reads.
Melchers F. Biosynthesis of the carbohydrate portion of immunoglobulin. Radiochemical and chemical analysis of the carbohydrate moieties of two myeloma proteins purified from different subcellular fractions of plasma cells.
Biochemistry. Feb 16; 10 (4)– Melchers F. Biosynthesis of the carbohydrate portion of by: The carbohydrate structure and complete amino acid sequence of a human lambda-type immunoglobulin light chain, protein Sm lambda has been determined.
Structure of the Carbohydrate Units of IgE Immunoglobulin I. OVER-ALL COMPOSITION, GLYCOPEPTIDE ISOLATION, AND STRUCTURE OF THE HIGH MANNOSE OLIGOSACCHARIDE UNIT* (Received for publication, August 6, ) JACQUES BAENZIGER$ AND STUART KORNFELDQ. Asparagine-linked sugar chains were quantitatively released as oligosaccharides from human IgG2 and IgG4 myeloma proteins by hydrazinolysis followed byN-acetylation and NaB3H4 reduction.
Each oligosaccharide was isolated by serial lectin column chromatography. Study of their structures by sequential exoglycosidase digestion and methylation analysis, revealed that all of them Cited by: Flow diagram for the labeling of the carbohydrate moieties of immunoglobulins, i M sodium acetate, M sodium chloride, % sodium azide, pH z For details on oxidation conditions see text.
3 When using amino-containing reporter molecules, acetate buffer can be replaced with a buffer of choice. can be made depending on the degree of oxidation and labeling required and the type of Cited by: 1. Introduction. Glycosylation represents a major post-translational modification of proteins that can influence their structure and function.
All immunoglobulins are glycosylated, and the amount of carbohydrate present and the nature of glycosylation are characteristic of each immunoglobulin class.
The two main types of oligosaccharide linkages to the protein are the N-linked and O-linked Cited by: No evidence was found for abnormalities of N-linked glycosylation of either isotype in IgA nephropathy compared with matched controls. However, in IgA nephropathy, reduced terminal galactosylation of the hinge region O-linked moieties was demonstrated; this was not seen in C1 inhibitor, which showed normal or increased galactosylation of the O Cited by: Structural study of the carbohydrate moieties of two human immunoglobulin subclasses (IgG2 and IgG4).
Glycoconjugate Journal6 (1), DOI: /BF Fumito Yamazaki, Tomoo Nukada, Yukishige Ito, Susumu Sato, Tomoya by: Evidence indicates that the carbohydrate moieties of IgG glycoproteins critically affect their antibody functions, particularly the effector functions mediated by the interactions with Fcγ.
Carbohydrate Moieties of Microsporidian Polar Tube Proteins Are Targeted by Immunoglobulin G in Immunocompetent Individuals. On this basis a predominance of multi-antennary structures was observed in the more glycosylated pathological immunoglobulins M (10% carbohydrate content), whereas oligomannosidic structures were increased in pathological immunoglobulins M with a lower content of carbohydrates Cited by: PDF | The T-cell receptor recognizes peptides bound to the major histocompatibility complex antigens.
Synthetic peptides corresponding to microbial | Find, read and cite all the research you. Presentation of immunogenic carbohydrate moieties to the epithelial surface of the gut in general does not elicit systemic IgG antibody responses. In AIDS patients worldwide E.
intestinalis is the predominant opportunistic infecting Encephalitozoon species, and E. cuniculi infection has been reported only infrequently (13, 30).Cited by: This study was designed to determine the time in the intracellular life of immunoglobulin when the carbohydrate moieties are added.
Plasma cells from a mouse myeloma tumor were exposed to glucosamine-3 H (a "bridge" sugar), galactose-3 H, or leucine-3 each of the above isotopes, the percentage of total radioactive immunoglobulin that has been secreted after different periods of Cited by: Abstract.
Immunoglobulin G (IgG) is a major serum glycoprotein that exerts the role of antibody in the immune system. This multifunctional glycoprotein couples antigen recognition with a variety of effector functions promoted via interactions with various IgG-binding proteins.
Given its versatile functionality, IgG has recently been used for therapeutic : Hirokazu Yagi, Saeko Yanaka, Koichi Kato. Carbohydrate Moieties of Microsporidian Polar Tube Proteins Are Targeted by Immunoglobulin G in Immunocompetent Individuals January Infection and Immunity 73(12)CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): This study was designed to determine the time in the intracellular life of immunoglobulin when the carbohydrate moieties are added.
Plasma cells from a mouse myeloma tumor were exposed to glucosamine- 3 H (a "bridge " sugar), galactose-3H, or leucine3H. With each of the above isotopes, the percentage of total.Advances in Carbohydrate Chemistry and Biochemistry has provided, since its inception incritical and informative articles written by research specialists that integrate the industrial, analytical, and technological aspects of biochemistry, organic chemistry, and instrumentation methodology to the study of carbohydrates.
Its articles present a definitive interpretation of the current Missing: immunoglobulin.