Esterase and protease activity of purified guinea pig basophil granules.

Highly purified granules of circulating guinea pig basophilic leukocytes were extracted with 0.1% Triton X-100 to yield a mixture of esterases-proteases including caseinolytic activity. By selective inhibition both trypsin- and chymotrypsin-like serine hydrolases have been identified. Sigmoidal pH dependences for hydrolysis of p-tosyl-L-arginine-methyl ester and N-benzoyl-L-tryosine-ethyl ester were observed for both intact granules and Triton granule extracts. Preliminary studies indicate that the enzymes are not solubilized even after Triton X-100 treatment of the granules.