Abstract
The effect of cleavage of Cl-inhibitor at Pro36 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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
