Abstract
Bradykinin is inactivated in one circulation through the intact or “blood-free rat lung (1). Inactivation of bradykinin occurs by hydrolysis of peptide bonds, yet the effluent of a blood-free lung preparation does not contain sufficient hydrolase activity to account for this extremely rapid and efficient degradation. Furthermore, there is no measurable retention of bradykinin or its peptide fragments by the lung. It seems likely, therefore, that bradykinin is inactivated by cellular enzymes at or near the endothelium of pulmonary blood vessels.
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© 1970 Plenum Press, New York
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Smith, U., Ryan, J.W. (1970). An Electron Microscopic Study of the Vascular Endothelium as a Site for Bradykinin and Adenosine-5′-Triphosphate Inactivation in Rat Lung. In: Sicuteri, F., e Silva, M.R., Back, N. (eds) Bradykinin and Related Kinins. Advances in Experimental Medicine and Biology, vol 8. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3198-8_31
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DOI: https://doi.org/10.1007/978-1-4684-3198-8_31
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