Yagi A, Harada N, Yamada H, Iwadare S, Nishioka I
J Pharm Sci. 1982 Oct;71(10):1172-4. doi: 10.1002/jps.2600711024.
A material having antibradykinin activity on isolated guinea pig ileum was partially purified from the nondialysate of the pulp of Aloe saponaria by repetition of gel chromatography using a hydrophilic polyvinyl gel and dextran gels. From the results of amino acid and carbohydrate analyses, the antibradykinin-active material was estimated to be a glycoprotein. It was found that this material catalyzes the hydrolysis of bradykinin at pH 7.4. The results of peptide analysis using reversed-phase high-performance liquid chromatography coupled with amino acid analysis indicate that this glycoprotein cleaves the Gly4-Phe5 and Pro7-Phe8 bonds of the bradykinin molecule.
