Abstract |
In half of the sera from patients with acute bacterial infections and 15% of the sera from patients with acute viral infections glycoproteins were found that form a scalariform pattern in the cationic range upon isoelectric focusing. The cationic glycoproteins appeared with the clinical illness. After subsidence of the symptoms they disappeared within 4 to 6 weeks. The proteins were identified as immunoglobulin G ( IgG) by determination of the NH2-terminal amino acid sequence. Remarkably, these IgG only contained light chains of the kappa type with high proportions of carbohydrates. Both, N-glycosidic- and O-glycosidic-bound glycans were present. The glycosylated light chains may render the cationic IgG multireactive. Thus, it may be part of an early nonspecific immune defense mechanism.
|
Authors | K Ritter, A Wiebusch, M Mäder, H Eiffert, H Kratzin, R Thomssen |
Journal | Medical microbiology and immunology
(Med Microbiol Immunol)
Vol. 182
Issue 3
Pg. 107-17
(Jul 1993)
ISSN: 0300-8584 [Print] Germany |
PMID | 8232066
(Publication Type: Journal Article)
|
Chemical References |
- Cations
- Glycoproteins
- Immunoglobulin G
- Immunoglobulin Light Chains
- Immunoglobulin kappa-Chains
|
Topics |
- Acute Disease
- Amino Acid Sequence
- Bacterial Infections
(blood, immunology)
- Cations
- Glycoproteins
(blood)
- Glycosylation
- Humans
- Immunoglobulin G
(isolation & purification)
- Immunoglobulin Light Chains
(isolation & purification)
- Immunoglobulin kappa-Chains
(isolation & purification)
- Molecular Sequence Data
- Virus Diseases
(blood, immunology)
|