Large cytoplasmic inclusion body kappa-chain has unusual intrachain disulfide bonding.
The Ig kappa L chain synthesized by the mouse hybridoma line F10 forms large fibrils in the lumen of the endoplasmic reticulum. Despite the formation of these inclusion bodies, free kappa-chain is secreted. Both intracellular and secreted kappa-chains in this line migrate faster on SDS gels; thus, the F10 kappa-chain seems to be more compact than normal Ig L chain. In normal kappa-chain, four cysteine residues form intrachain disulfide bonds and the fifth connects the L chain to the H chain. Although the five cysteine residues of the aberrant kappa-chain are in the normal positions, they display an unusual gel pattern when the intrachain disulfide bonds are opened with 2-ME; that is, the intrachain disulfide bonding pattern of F10 kappa-chain seems to be unusual. It is suggested that the abnormal folding pattern favors fibril formation.[1]References
- Large cytoplasmic inclusion body kappa-chain has unusual intrachain disulfide bonding. Jäck, H.M., Sloan, B., Grisham, G., Reason, D., Wabl, M. J. Immunol. (1993) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
