Abstract
Incubation of heat-denatured plasma from the reticulated python, Python reticulatus with trypsin generated bradykinin-like immunoreactivity which was detected by radioimmunoassay using an antiserum raised against mammalian bradykinin. The primary structure of python bradykinin was established as Ala-Pro-Pre-Gly-Phe-Thr-Pro-Phe-Arg. This amino acid sequence contains two substitutions (Arg1 → Ala and Ser6 → Thr) compared with mammalian bradykinin. Treatment of python plasma with glass beads under conditions previously shown to generate [Thr6]bradykinin in the plasma of a turtle and an alligator did not generate bradykinin-like immunoreactivity. The data indicate that the plasma of a lepidosaur contains a kininogen but, unlike the plasma of chelonians and crocodilians, does not contain a prekallikrein activator related to Factor XII. © 1994 by Academic Press, Inc.
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CITATION STYLE
Conlon, J. M., & Lance, V. A. (1994). Generation of [Ala1, Thr6]Bradykinin in the Plasma of a Snake, the Reticulated Python. General and Comparative Endocrinology, 94(2), 273–278. https://doi.org/10.1006/gcen.1994.1083
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