Disulfide linkages between antigen-binding receptors on chicken B-lymphocytes Journal Article


Authors: Rosenspire, A. J.; Myung Soo, Lee; Pollak, S. V.; Yong Sung, Choi
Article Title: Disulfide linkages between antigen-binding receptors on chicken B-lymphocytes
Abstract: Membrane immunoglobulin receptors on chicken B-cells have been shown to display a heterogeneity with respect to interchain disulfide linkages. One fraction of the surface Ig (sIg) appears to display the traditional H2-L2 linkage. We also present evidence that this Ig is covalently bound via a disulfide linkage to actin. In this instance, the isolated Ig heavy chain, after reduction, has a mol. wt of 80 K. Perhaps more significantly, we show that another fraction of the sIg exists in a highly aggregated form that is stabilized by disulfide linkages. In contrast to the sIg found in the H2-L2 configuration, there is no evidence of actin within the aggregates and the sIg heavy chains isolated from these aggregates display a slightly faster mobility on SDS-PAGE under reducing conditions, running at about 77 K. Furthermore, it appears that the Ig within the large aggregates may have a higher avidity with respect to antigen binding, and so this Ig structure may be the more relevant to antigen-induced receptor-mediated signaling in the B-cell. © 1986.
Keywords: nonhuman; animal; actin; spleen; b lymphocyte; b-lymphocytes; lymphatic system; molecular weight; disulfide; disulfides; electrophoresis, polyacrylamide gel; chickens; receptors, antigen, b-cell; immunoglobulin receptor; chicken; chromatography, affinity; priority journal; support, u.s. gov't, p.h.s.; immunoglobulins, heavy-chain; immunoglobulins, surface
Journal Title: Molecular Immunology
Volume: 23
Issue: 1
ISSN: 0161-5890
Publisher: Pergamon-Elsevier Science Ltd  
Date Published: 1986-01-01
Start Page: 1
End Page: 13
Language: English
DOI: 10.1016/0161-5890(86)90166-5
PUBMED: 3083239
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 18 August 2021 -- Source: Scopus
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