Abstract
1. The isolated lungs of guinea-pigs, rats and dogs, perfused with Krebs bicarbonate solution via the pulmonary artery, inactivated 95, 98 and 99% respectively of the bradykinin infused through them.
2. This inactivation process was not inhibited by 2-mercaptoethanol (1 mM) or EDTA (500 μM).
3. The inactivation was inhibited by 2:3-dimercaptopropanol (100 μM), N-ethylmaleimide (100 μM), and several of the bradykinin potentiating peptides from Bothrops jararaca, in both natural and synthetic forms.
4. The effect of these compounds, 2-mercaptoethanol, EDTA, 2:3-dimercaptopropanol, N-ethylmaleimide and Bothrops peptides on the pulmonary bradykininase activity is the same as their effect on pulmonary angiotensin I converting enzyme.
Full text
PDF











Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Alabaster V. A., Bakhle Y. S. Removal of 5-hydroxytryptamine in the pulmonary circulation of rat isolated lungs. Br J Pharmacol. 1970 Nov;40(3):468–482. [PMC free article] [PubMed] [Google Scholar]
- BUMPUS F. M., SMEBY R. R., PAGE I. H., KHAIRALLAH P. A. DISTRIBUTION AND METABOLIC FATE OF ANGIOTENSIN II AND VARIOUS DERIVATIVES. Can Med Assoc J. 1964 Jan 25;90:190–193. [PMC free article] [PubMed] [Google Scholar]
- Bakhle Y. S. Conversion of angiotensin I to angiotensin II by cell-free extracts of dog lung. Nature. 1968 Nov 30;220(5170):919–921. doi: 10.1038/220919a0. [DOI] [PubMed] [Google Scholar]
- Bakhle Y. S. Inhibition of angiotensin I converting enzyme by venom peptides. Br J Pharmacol. 1971 Sep;43(1):252–254. doi: 10.1111/j.1476-5381.1971.tb07176.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bakhle Y. S., Reynard A. M. Characteristics of the angiotensin I converting enzyme from dog lung. Nat New Biol. 1971 Feb 10;229(6):187–189. doi: 10.1038/newbio229187a0. [DOI] [PubMed] [Google Scholar]
- Bakhle Y. S., Reynard A. M., Vane J. R. Metabolism of the angiotensins in isolated perfused tissues. Nature. 1969 Jun 7;222(5197):956–959. doi: 10.1038/222956a0. [DOI] [PubMed] [Google Scholar]
- Biron P. Pulmonary extractionof bradykinin and eledoisin. Rev Can Biol. 1968 Mar;27(1):75–76. [PubMed] [Google Scholar]
- ERDOS E. G., SLOANE E. M. An enzyme in human blood plasma that inactivates bradykinin and kallidins. Biochem Pharmacol. 1962 Jul;11:585–592. doi: 10.1016/0006-2952(62)90119-3. [DOI] [PubMed] [Google Scholar]
- FERREIRA S. H. A BRADYKININ-POTENTIATING FACTOR (BPF) PRESENT IN THE VENOM OF BOTHROPS JARARCA. Br J Pharmacol Chemother. 1965 Feb;24:163–169. doi: 10.1111/j.1476-5381.1965.tb02091.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ferreira S. H., Bartelt D. C., Greene L. J. Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry. 1970 Jun 23;9(13):2583–2593. doi: 10.1021/bi00815a005. [DOI] [PubMed] [Google Scholar]
- Ferreira S. H., Rocha e Silva M. Potentiation of bradykinin and eledoisin by BPF (bradykinin potentiating factor) from Bothrops jararaca venom. Experientia. 1965 Jun 15;21(6):347–349. doi: 10.1007/BF02144709. [DOI] [PubMed] [Google Scholar]
- Ferreira S. H., Vane J. R. The detection and estimation of bradykinin in the circulating blood. Br J Pharmacol Chemother. 1967 Mar;29(3):367–377. doi: 10.1111/j.1476-5381.1967.tb01968.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ferreira S. H., Vane J. R. The disappearance of bradykinin and eledoisin in the circulation and vascular beds of the cat. Br J Pharmacol Chemother. 1967 Jun;30(2):417–424. doi: 10.1111/j.1476-5381.1967.tb02148.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gruby L. A., Rowlands C., Varley B. Q., Wyllie J. H. The fate of 5-hydroxytryptamine in the lungs. Br J Surg. 1971 Jul;58(7):525–532. doi: 10.1002/bjs.1800580716. [DOI] [PubMed] [Google Scholar]
- Iwata H., Shikimi T., Oka T. Pharmacological significances of peptidase and proteinase in the brain. I. Enzymatic inactivation of bradykinin in rat brain. Biochem Pharmacol. 1969 Jan;18(1):119–128. doi: 10.1016/0006-2952(69)90016-1. [DOI] [PubMed] [Google Scholar]
- MANN M., WEST G. B. The nature of hepatic and splenic sympathin. Br J Pharmacol Chemother. 1950 Jun;5(2):173–177. doi: 10.1111/j.1476-5381.1950.tb01004.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Piper P. J., Vane J. R. Release of additional factors in anaphylaxis and its antagonism by anti-inflammatory drugs. Nature. 1969 Jul 5;223(5201):29–35. doi: 10.1038/223029a0. [DOI] [PubMed] [Google Scholar]
- Pojda S. M., Vane J. R. Inhibitory effects of aprotinin on kallikrein and kininases in dog's blood. Br J Pharmacol. 1971 Aug;42(4):558–568. doi: 10.1111/j.1476-5381.1971.tb07140.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ryan J. W., Roblero J., Stewart J. M. Inactivation of bradykinin in the pulmonary circulation. Biochem J. 1968 Dec;110(4):795–797. doi: 10.1042/bj1100795. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Scholz H. W., Biron P. Non-identity between pulmonary bradykininase and converting-enzyme activity. Rev Can Biol. 1969 Sep;28(3):197–200. [PubMed] [Google Scholar]
- Suzuki K., Abinko T., Endo N., Kameyama T., Sasaki K. Biologically active synthetic fragments of bradykinin. Jpn J Pharmacol. 1969 Jun;19(2):325–327. doi: 10.1254/jjp.19.325. [DOI] [PubMed] [Google Scholar]
- Yang H. Y., Erdös E. G., Levin Y. Characterization of a dipeptide hydrolase (kininase II: angiotensin I converting enzyme). J Pharmacol Exp Ther. 1971 Apr;177(1):291–300. [PubMed] [Google Scholar]
- Yang H. Y., Erdös E. G. Second kininase in human blood plasma. Nature. 1967 Sep 23;215(5108):1402–1403. doi: 10.1038/2151402a0. [DOI] [PubMed] [Google Scholar]
