Journal of Experimental Medicine, Vol 153, 1672-1677, Copyright © 1981 by Rockefeller University Press
Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor
M Taniguchi, T Saito, I Takei and T Tokuhisa
The secreted form of the suppressor T cell factor specific for keyhole
limpet hemocyanin derived from the hybridoma 34S-704 was found to consist
of the two distinct polypeptide chains, i.e., the antigen- binding and the
I-J-encoded chains. They were linked in covalent association with disulfide
bonds. The two chains were cleaved by the reduction with dithiothreitol and
were easy to reconstitute the active form of TsF. The association of the
two distinct chains was suggested to be essential for the expression of the
TsF activity.
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