منابع مشابه
Human serum IgM glycosylation: identification of glycoforms that can bind to mannan-binding lectin.
The glycoprotein IgM is the major antibody produced in the primary immune response to antigens, circulating in the serum both as a pentamer and a hexamer. Pentameric IgM has a single J chain, which is absent in the hexamer. The mu (heavy) chain of IgM has five N-linked glycosylation sites. Asn-171, Asn-332, and Asn-395 are occupied by complex glycans, whereas Asn-402 and Asn-563 are occupied by...
متن کاملSerum IgM and IgA
SYNOPSIS Immunofluorescent serum IgM and/or a significant level of IgA antibody was detected in 87 % of 39 cases of current or recent influenza A infection from two to 84 days after the onset of illness. Secondary IgM staining occurred in 5% of sera and a significant correlation was found between complement-fixing and class-specific antibodies. It was estimated that the immunofluorescent test c...
متن کاملNormal human serum contains a natural IgM antibody cytotoxic for human neuroblastoma cells.
Neuroblastoma (NB) is characterized by the second highest spontaneous regression of any human malignant disorder, a phenomenon that remains to be elucidated. In this study, a survey of 94 normal human adult sera revealed a considerable natural humoral cytotoxicity against human NB cell lines in approximately one-third of the tested sera of both genders. Specific cell killing by these sera was i...
متن کاملSerum IgM antibody and influenza A infection.
Sucrose density gradient ultracentrifugation followed by haemagglutination inhibition for demonstrating specific influenza IgM was evaluated as a means of confirming recent infection with influenza A viruses. Specific IgM antibodies were found in at least one serum obtained from 83% of patients with proven recent infection with influenza A viruses but in none of the sera from 21 individuals wit...
متن کاملA Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
We demonstrate a new approach for the site-specific identification and characterization of protein N-glycosylation. It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions. A chromatographic separation of a proteolytic digest is deposited at a high frequency on the microa...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2005
ISSN: 0021-9258
DOI: 10.1074/jbc.m504528200