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Abstract
Abstract The factor in ovine iso-immune L-antiserum that was responsible for stimulation of active K+-transport in LK sheep red cells was found to be an antibody of the IgG1 class. Reduction and alkylation of the anti-L-IgG1 protein abolished its K+-pump stimulatory activity. Treatment with papain to yield univalent Fab fragments substantially reduced stimulatory activity; there was no enhancement from the Fc protein. Bivalent fragments obtained by pepsin digestion, however, were nearly fully active in effecting stimulation of active K+-transport in LK sheep red cells.
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