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.
Original language | English |
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Pages (from-to) | 273-278 |
Number of pages | 6 |
Journal | General and Comparative Endocrinology |
Volume | 94 |
Issue number | 2 |
DOIs | |
Publication status | Published - May 1994 |
Externally published | Yes |
ASJC Scopus subject areas
- Animal Science and Zoology
- Endocrinology