Therehas longbeenconjectureover thedegree towhichthere may be structural and functional heterogeneity in the tetra-mericserineproteasetryptase(EC ), amajor mediator of allergic inflammation. We have applied 2D gel electrophoresis to analyze the extent, nature, and variability of thisheterogeneity inlysatesofmast cells isolatedfromlung and skin, and in preparations of purified tryptase. Gels were silver stained, or the proteins transferred to nitrocellulose blots and probed with either tryptase-specific monoclonal antibodies or various lectins. .
