Comparative Analysis of a Monoclonal Antigen-Specific T Suppressor Factor Obtained from Supernatant, Membrane or Cytosol of a T-Cell Hybridoma
Our previous studies (1,2) have shown the purification to chemical homogeneity of a monoclonal, GAT-specific T suppressor cell factor (TsF1) obtained from the supernatant of a T-cell hybridoma. This suppressor factor is unique compared to other antigen-specific suppressor factors in terms of its size (24–29,000 M.W.); its structure (1 polypeptide chain); and the presence of an antigen binding site and I region determinant on the one polypeptide. Since the original report we have purified several other monoclonal antigen-specific suppressors all of which have the same general characteristics (Gerassi et al., submitted for publication; Healy et al., submitted for publication; Sorensen et al., submitted for publication; 3,4). These results suggest that these single chain suppressor factors represent a discrete family which we have termed TsF1 due to their biochemical and biological properties (see Kapp et al., this volume). The unit size of the TsF1 molecules has been confirmed by translating TsF1 mRNA in a rabbit reticulocyte lysate system and determining the size of the product (5). The minimum size obtained in these studies is 19–28,000 M.W.
KeywordsHigh Pressure Liquid Chromatography Chemical Homogeneity Antigen Binding Site Suppressor Factor Molecular Weight Form
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