Abstract
The effect of cleavage of Cl-inhibitor at Pro 36 by a Crotalus atrox α-proteinase fraction on the properties of this serpin was studied. This truncated Cl-inhibitor (des 1–36) was fully active as an inhibitor of kallikrein, β-factor XIIa, and Cl̄s, and modulated the functions of Cl in a normal manner. Also, the half-life of the truncated protein in the circulation of rabbits, both alone and in complex with Cl̄, was not altered. These results show that shock-like symptoms caused by C. atrox envenomation are not attributable to a deficiency in Cl-inhibitor caused by the action of the metalloproteinase in the α-proteinase fraction.
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